Tokushima University / Educator and Researcher Directory --- Gotoh, Toshio

Field of Study

○	Comparative Physiology and Biochemistry

Subject of Study

○	環形動物巨大ヘモグロビンの分子構築と進化, フィブリン安定化因子の構造と機能 (hemoglobin, erythrocruorin, Annelids, molecular architecture of protein, molecular evolution, fibrin stabilizing factor, blood clotting factor XIII)

Book / Paper

Academic Paper (Judged Full Paper):

1.	Kanako Waki, Akiko Noami, Mikiko Hashimoto, Akio Okuma, Ituka Kubo, Taku Kanai, Takanori Satoh, Minoru Watanabe and Toshio Gotoh : Novel S-S loops in the globin chains from the giant hemoglobin of the polychaete Perinereis aibuhitensis., Natural Science Research, Vol.22, 105-125, 2008. (Tokushima University Institutional Repository) ● Metadata: 62134 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1050020697878137472 (Tokushima University Institutional Repository: 62134, CiNii: 1050020697878137472)
2.	Takayuki K. Nemoto, Toshio Ono, Takeshi Kobayakawa, Tanaka Etsuko, Ki-ichiro Tanaka, Takashi Takagi and Toshio Gotoh : Domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90 molecular chaperone, European Journal of Biochemistry, Vol.268, No.20, 5258-5269, 2001. (Summary) In the present study, we investigated the domain structure and domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90. Limited proteolysis of recombinant HtpG, revealed three major tryptic sites, i.e. Arg7-Gly8, Arg336-Glu337 and Lys552-Leu553, of which the latter two were located at the positions equivalent to the major cleavage sites of human HSP90alpha. A similar pattern was obtained by papain treatment under nondenaturing conditions but not under denaturing conditions. Thus, HtpG consists of three domains, i.e. Domain A, Met1-Arg336; domain B, Glu337-Lys552; and domain C, Leu553-Ser624, as does HSP90. The domains of HtpG were expressed and their interactions were estimated on polyacrylamide gel electrophoresis under nondenaturing conditions. As a result, two kinds of domain-domain interactions were revealed: domain B interaction with domain A of the same polypeptide and domain C of one partner with domain B of the other in the dimer. Domain B could be structurally and functionally divided into two subdomains, the N-terminal two-thirds (subdomain BI) that interacted with domain A and the C-terminal one-third (subdomain BII) that interacted with domain C. The C-terminal two-thirds of domain A, i.e. Asp116-Arg336, were sufficient for the binding to domain B. We finally propose the domain organization of an HtpG dimer. (Keyword) Amino Acid Sequence / Bacterial Proteins / Dimerization / Electrophoresis, Gel, Two-Dimensional / Electrophoresis, Polyacrylamide Gel / Escherichia coli / Escherichia coli Proteins / HSP90 Heat-Shock Proteins / Histidine / Molecular Sequence Data / Molecular Weight / Papain / Peptide Fragments / Peptides / Protein Binding / Protein Interaction Mapping / Protein Structure, Tertiary / Recombinant Proteins / Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Substrate Specificity / Trypsin (Link to Publication Site) ● Publication site (DOI): 10.1046/j.0014-2956.2001.02457.x (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 11606187 ● Summary page in Scopus @ Elsevier: 2-s2.0-0034792056 (DOI: 10.1046/j.0014-2956.2001.02457.x, PubMed: 11606187, Elsevier: Scopus)
3.	Brian N. Green, Toshio Gotoh, Tomohiko Suzuki, Franck Zal, Francois H. Lallier, Andre Toulmond and Serge N. Vinogradov : Electrospray Ionization Mass Spectrometric Observation of Large, Noncovalent Globin Subassemblies in the ~3600 kDa Hexagonal Bilayer Hemoglobins, Journal of Molecular Biology, Vol.309, 553-560, 2001.
4.	Masaya Satoh, Emi Karaki, Mamiko Kakehashi, Eisuke Okazaki, Toshio Gotoh and Yasuo Oyama : Heavy-metal induced changes in cellular nonproteinaceous thiol levels and heavy metal-binding peptides in Tetraselmis tetrathele (Prasinophyceae), Journal of Phycology, Vol.35, 989-994, 1999. (Summary) The effects of mercury and cadmium on the intracellular level of nonprotein thiols in a unicellular green alga Tetraselmis tetrathele (Prasinophyceae) were investigated by using a fluorescent dye, 5-chloromethylfluorescein (5CMF), as a probe for nonprotein thiols. Depletion of nonprotein thiols began within 30 min, and completely depleted at 2 h, and most cells died at 24 h after exposure the cells to more than 3.0 M HgCl2. HPLC analyses revealed that glutathione was a major nonprotein thiol in T. tetrathele. A tripeptide, Arg-Arg-Glu, was found to be abundant and it showed ability to bind Hg2+, suggesting that it functions to scavenge heavy metals as well as thiol molecules.
5.	Mariko Yamaki, Kenji Kubota, Keiko Matsubara, Satoshi Ebina and Toshio Gotoh : Carbohydrate-gluing is a strategy for supramolecular clamping of submutiples in annelid extracellular multi-subunit hemoglobin, Archives of Biochemistry and Biophysics, Vol.355, No.1, 119-123, 1998. (Summary) A key to understanding the mysterious hierarchic organization of annelid multi-subunit extracellular hemoglobin (giant Hb, composed of 144 globin chains and about 36 nonheme chains called linkers) is knowing the role of linkers in holding together the entire two-tiered hexagonal form. Here, the effects of added monosaccharides on the dissociation of giant Hb from the marineworm Perinereis aibuhitensis were monitored using dynamic light scattering (DLS), transmission electron microscopy (TEM), and circular dichroism (CD) measurements. Changes in Stokes radius and more clearly the distribution analysis of the Hb based on the DLS measurements showed that Hb preferentially dissociates into hexagonal units (called submultiples), which was consistent with the results of TEM and CD measurements. The results thus show that linkers specifically "clamp" submultiples together to organize the two-tiered form through carbohydrate gluing. Thus, a submultiple behaves like an ordinary protein, whereas the intact Hb behaves like a miniature supramolecular system. This clamp model is plausible because it inherently involves catastrophe of the molecular stoichiometry at the two-tiered hexagonal formation level because carbohydrates are under posttranslational regulation and therefore contain structural ambiguity. (Keyword) Animals / Carbohydrates / Circular Dichroism / Globins / Heme / Hemoglobins / Light / Macromolecular Substances / Microscopy, Electron / Polychaeta / Protein Conformation / Protein Structure, Secondary / Scattering, Radiation (Link to Publication Site) ● Publication site (DOI): 10.1006/abbi.1998.0705 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 9647674 ● Summary page in Scopus @ Elsevier: 2-s2.0-0032126970 (DOI: 10.1006/abbi.1998.0705, PubMed: 9647674, Elsevier: Scopus)
6.	Toshio Gotoh, Toshiya Sano, Akihiro Shibuya, Mariko Yamaki, Kiyohiro Imai and Satoshi Ebina : Hexagonal bilayer structuring activity of linker chains of an annelid giant hemoglobin from the polychaete Perinereis aibuhitensis, Archives of Biochemistry and Biophysics, Vol.360, 75-84, 1998.
7.	Keiko Matsubara, Mariko Yamaki, Kuniaki Nagayama, Kiyohiro Imai, Hiroyoshi Ishi, Toshio Gotoh and Satoshi Ebina : Wheat germ agglutinin-reactive chains of giant hemoglobin from the polychaete Perinereis aibuhitensis., Biochimica et Biophysica Acta (BBA) - General Subjects, Vol.1290, No.3, 215-223, 1996. (Summary) Wheat germ agglutinin-reactive chains of multisubunit extracellular hemoglobin from the polychaete Perinereis aibuhitensis were identified to clarify the carbohydrate gluing which is the carbohydrate-dependent supramolecular architecture of the hemoglobin (Ebina S. et al. (1995) Proc. Natl. Acad. Sci. USA 92, 7367-7371). Electron microscope micrographs of Perinereis hemoglobin showed a characteristic shape of two-tiered hexagonal rings whose diameter and height were determined to be 29.4 +/- 1.7 nm and 20.0 +/- 1.8 nm, respectively. Four types of globins and two types of linkers were isolated from the giant hemoglobin by reverse-phase chromatography and SDS-PAGE. These constituents showed similar NH2-terminal sequences as those previously reported for corresponding chains of Tylorrhynchus hemoglobin (Suzuki T. and Gotoh T. (1986) J. Biol. Chem. 261, 9257-9267; Suzuki T. et al. (1990) J. Biol. Chem. 265, 12168-12177). Thus, each globin of Perinereis hemoglobin was identified in terms of amino acid sequence homology and designated using names common to Tylorrhynchus hemoglobin, namely, a, A, b, and B. The linkers were stained by horseradish peroxidase (HRP)-lectins and PAS staining kits, indicating the presence of carbohydrate oligomers. Lectin staining was also significantly positive to globins a and A, which belong to strain A, but negative to globins b and B, which belong to strain B. Results showed that linkers and globins of strain A had a site in a carbohydrate oligomer to which wheat germ agglutinin (WGA) could bind. On the other hand, an alignment between known amino acid sequences of annelid globins and linkers and the sequences of lectins revealed that only the domain of the cysteine-rich motif in linkers has a homology with WGA-type lectins. The results of this study clarify the structuring mechanism of a supramolecule by lectin-like binding, called carbohydrate gluing. (Keyword) Amino Acid Sequence / Animals / Carbohydrate Sequence / Carbohydrates / Glycoproteins / Hemoglobins / Molecular Sequence Data / Molecular Weight / Polychaeta / Protein Binding / Sequence Analysis / Staining and Labeling / Wheat Germ Agglutinins (Link to Publication Site) ● Publication site (DOI): 10.1016/0304-4165(96)00010-4 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 8765123 ● Search Scopus @ Elsevier (PMID): 8765123 ● Search Scopus @ Elsevier (DOI): 10.1016/0304-4165(96)00010-4 (DOI: 10.1016/0304-4165(96)00010-4, PubMed: 8765123)
8.	Mariko Yamaki, Keiko Matsubara, Akihiro Shibuya, Toshio Gotoh and Satoshi Ebina : Identification of the subunit loci in the extracellular multisubunit hemoglobin from annelid Perinereis aibuhitensis., Archives of Biochemistry and Biophysics, Vol.335, 23-31, 1996.
9.	Brian N Green, Tomohiko Suzuki, Toshio Gotoh, Askar R Kuchumov and Serge N Vinogradov : Electrospray ionization mass spectrometric determination of the complete polypeptide chain composition of Tylorrhynchus heterochaetus hemoglobin., The Journal of Biological Chemistry, Vol.270, No.31, 18209-18211, 1995.
10.	Satoshi Ebina, Keiko Matsubara, Kuniaki Nagayama, Mariko Yamaki and Toshio Gotoh : Carbohydrate gluing, an architectural mechanism in the supramolecular structure of an annelid gaint hemoglobin., Proceedings of the National Academy of Sciences of the United States of America, Vol.92, No.16, 7367-7371, 1995.
11.	Tomohiko Suzuki, Takashi Takagi and Toshio Gotoh : Primary structure of two linker chains of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus., The Journal of Biological Chemistry, Vol.265, 12168-12177, 1990.
12.	Toshio Gotoh and Tomohiko Suzuki : Molecular assembly and evolution of multi-subunit extracxellular annelid hemoglobins., Zoological Science, Vol.7, 1-16, 1990.
13.	A. Tsuneshige, K. Imai, I. Tyuma and Toshio Gotoh : Spectrophotometric, electron paramagnetic resonance and oxygen binding studies on the hemoglobin from the marine polychaete Perinereis aibuhitensis (Grube): comparative physiology of hemoglobin., The Journal of Biochemistry, Vol.106, 406-417, 1989.
14.	James J. Lightbody, Aziz N. Quasba, Mark G. Mainwaring, James S. Young, Daniel A. Walz, Serge N. Vinogradov and Toshio Gotoh : Immunological relatedness of annelid extracellular hemoglobins and chlorocruorins., Comparative Biochemistry and Physiology, Vol.90B, No.2, 301-305, 1988.
15.	I. Pilz, E. Schwarz, Tomohiko Suzuki and Toshio Gotoh : Small-angle X-ray scattering studies of annelid giant haemoglobin from Tylorrhynchus heterochaetus, Int. J. Biol. Macromol., Vol.10, 356-360, 1988.
16.	M. Goodman, J. Pedwadon, J. Czeluniak, Tomohiko Suzuki and Toshio Gotoh : An evolutionary tree for invertebrate globin sequences., Journal of Molecular Evolution, Vol.27, 119-123, 1988.
17.	Tomohiko Suzuki, O.H. Kapp and Toshio Gotoh : Novel S-S loops in the giant hemoglobin of Tylorrhynchus heterochaetus., The Journal of Biological Chemistry, Vol.263, 18524-18529, 1988.
18.	P.R Standley, M.G. Mainwaring, Toshio Gotoh and S.N. Vinogradov : The calcium, copper and zinc content of some annelid extracellular haemoglobins., The Biochemical Journal, Vol.249, No.3, 915-916, 1988.
19.	Fumio Shishikura, J.W. Snow, Toshio Gotoh, S.N. Vinogradov and D.A. Walz : Amino acid sequence of the monomer subunit of the extracellular hemoglobin of Lumbricus terrestris., The Journal of Biological Chemistry, Vol.262, 3123-3131, 1987.
20.	Toshio Gotoh, Fumio Shishikura, J.W. Snow, K.I. Ereifej, S.N. Vinogradov and DA Walz : Two globin strains in the giant annelid extracellular haemoglobins., The Biochemical Journal, Vol.241, No.2, 441-445, 1987.
21.	Tomohiko Suzuki and Toshio Gotoh : Subunit assembly of giant haemoglobin from the polychaete Tylorrhynchus heterochaetus., Journal of Molecular Biology, Vol.190, 119-123, 1986.
22.	J.J. Lightbody, E.L. Ziaja, S.D. Lugo, M.G. Mainwaring, S.N. Vinogradov, Fumio Shishikura, D.A. Walz and Toshio Gotoh : Preparation and characterization of monoclonal antibodies to the extracellular hemoglobin of Lumbricus terrestris., Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol.873, No.3, 340-349, 1986. (Summary) Murine monoclonal antibodies to the extracellular hemoglobin of Lumbricus terrestris were prepared by a modification of the method of Kohler and Milstein. 224 hybridomas were found to produce antibodies which bound to the hemoglobin; they were tested for binding to the four subunits of the hemoglobin: M (chain I, 16 kDa), D1 (chain V, 31 kDa), D2 (chain VI, 37 kDa) and T (50 kDa), a disulfide-bonded trimer of chains II, III and IV, each of about 17 kDa. 150 hybridomas bound to all four subunits and 40 hybridomas bound to various combinations of subunits. The remaining 34 hybridomas combined only with the hemoglobin. The twelve hybridomas obtained after subculturing and cloning were tested for their binding to the two fractions II and III, consisting of subunits D1 + D2 + T and M, respectively, obtained by dissociation at pH 9.5 and at pH 4.0 and to the reassociated whole molecules, obtained subsequent to return to neutral pH. Eight hybridomas which combined only with the hemoglobin also combined with all the reassociated molecules but not with any of the fractions: these monoclonal antibodies probably recognize conformation-dependent antigenic sites that are present only in the hexagonal bilayer structure characteristic of the native and reassociated hemoglobin molecules. Of the remaining four hybridomas, two bound to subunit T and two combined with subunits T and D2; they also combined with the reassociated molecules and with the fractions II. In addition, the hybridomas did not bind to the hemoglobins of Tubifex, Limnodrilus, Arenicola, Tylorrhynchus and Macrobdella or to the chlorocruorins of Myxicola and Eudistylia. (Keyword) Amino Acids / Animals / Antibodies, Monoclonal / Antibody Specificity / Enzyme-Linked Immunosorbent Assay / Hemoglobins / Mice / Mice, Inbred BALB C / Peptide Fragments / Polychaeta (Link to Publication Site) ● Publication site (DOI): 10.1016/0167-4838(86)90082-8 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 3756184 ● Search Scopus @ Elsevier (PMID): 3756184 ● Search Scopus @ Elsevier (DOI): 10.1016/0167-4838(86)90082-8 (DOI: 10.1016/0167-4838(86)90082-8, PubMed: 3756184)
23.	Tomohiko Suzuki, Takashi Takagi and Toshio Gotoh : Amino acid sequence of the smallest polypeptide chain containing heme of extra-cellular hemoglobin from the polychaete Tylorrhynchus heterochaetus., Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, Vol.708, No.3, 253-258, 1986. (Link to Publication Site) ● Publication site (DOI): 10.1016/0167-4838(82)90434-4 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/0167-4838(82)90434-4 (DOI: 10.1016/0167-4838(82)90434-4)
24.	Tomohiko Suzuki and Toshio Gotoh : The complete amino acid sequence of giant multisubunit hemoglobin from the polychaete Tylorrhynchus heterochaetus., The Journal of Biological Chemistry, Vol.261, 9257-9267, 1986.
25.	Toshio Gotoh, Mainwaring Mark, Fumio Shishikura, Daniel A. Walz and Serge N. Vinogrodov : Isolation of the subunits and polypeptide chains of the extracellular hemoglobin of Lumbricus terrestris., Biophysical Journal, Vol.49, No.2-2, 542a, 1986.
26.	Tomohiko Suzuki, H. Yasunaga, Takahiro Furukohri, Kenichi Nakamura and Toshio Gotoh : Amino ascid sequence of polypeptide chain IIB of extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus., The Journal of Biological Chemistry, Vol.260, 11481-11487, 1985.
27.	Tomohiko Suzuki, Takahiro Furukohri and Toshio Gotoh : Subunit structure of extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus and amino acid sequence of the constituent polypeptide chain (IIC)., The Journal of Biological Chemistry, Vol.260, 3145-3154, 1985.
28.	Tomohiko Suzuki, H. Murakami and Toshio Gotoh : Auto-deoxygenation of annelid giant haemoglobin in vitro., Int. J. Biol. Macromol., Vol.6, 226-228, 1984.
29.	Tomohiko Suzuki, Mutsuko Kobayashi, Takahiro Furukohri and Toshio Gotoh : Autoxidation of extracellular oxyhaemoglobin from the polychaete Perinereis brevicirris (Grube)., Comparative Biochemistry and Physiology, Vol.75B, No.1, 17-21, 1983.
30.	Tomohiko Suzuki, Takashi Takagi, Takahiro Furukohri and Toshio Gotoh : Separation of constituent polypeptide chains containing heme from extracellular hemoglobin of the polychaete Perinereis brevicirris (Grube)., Comparative Biochemistry and Physiology, Vol.75B, No.4, 567-570, 1983.
31.	Toshio Gotoh and Seiko Kamada : Subunit structure of erythrocruorin from the polychaete Tylorrhynchus heterochaetus., The Journal of Biochemistry, Vol.87, 557-562, 1980.
32.	Toshio Gotoh and Keiji Shikama : Generation of superoxide radical during the autoxidation of oxymyoglobin., The Journal of Biochemistry, Vol.80, 397-399, 1976.
33.	Toshio Gotoh and Keiji Shikama : Autoxidation of native oxymyoglobin from bovine heart muscle., Archives of Biochemistry and Biophysics, Vol.163, 476-481, 1974.
34.	Takehiko Ochiai, Toshio Gotoh and Keiji Shikama : Effect of intracellular organic phosphate on the oxygen equilibrium curve of chicken hemoglobin., Archives of Biochemistry and Biophysics, Vol.149, 316-322, 1972.
35.	Toshio Gotoh, Takehiko Ochiai and Keiji Shikama : Chromatographic separation of oxy- and met-myoglobin on a DEAE-cellulose column., Journal of Chromatography. A., Vol.60, No.2, 260-264, 1971. (Keyword) Animals / Cattle / Chromatography, DEAE-Cellulose / Hemoglobins / myocardium / Myoglobin / Oxygen (Link to Publication Site) ● Publication site (DOI): 10.1016/S0021-9673(00)95561-4 (Link to Search Site for Scientific Articles) ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 5096110 ● Summary page in Scopus @ Elsevier: 2-s2.0-0015241389 (DOI: 10.1016/S0021-9673(00)95561-4, PubMed: 5096110, Elsevier: Scopus)
36.	L. Lorand and Toshio Gotoh : Fibrinoligase: The fibrin stabilizing factor system., Methods in Enzymology, Vol.19, 770-782, 1970.
37.	L. Lorand, J. Downey, Toshio Gotoh, A. Jacobsen and Seiichi Tokura : The transpeptidase system which crosslinks fibrin by γ-glutamyl-ε-lysine bonds., Biochemical and Biophysical Research Communications, Vol.31, 222-230, 1968. (Link to Publication Site) ● Publication site (DOI): 10.1016/0006-291X(68)90734-1 (Link to Search Site for Scientific Articles) ● Search Scopus @ Elsevier (DOI): 10.1016/0006-291X(68)90734-1 (DOI: 10.1016/0006-291X(68)90734-1)

Academic Paper (Unrefereed Paper):

1.	Taku Kanai, Toshiya Sano, Takae Bandoh, Akihiro Kaneyama, Yuhko Nakanishi, Kanako Waki, Satoshi Murakami, Hisako Kuratomi, Wakako Tokunaga, Akihiro Shibuya, Tomoko Yamashita, Takanori Satoh and Toshio Gotoh : Reassociation of annelid giant hemoglobin from the polychaete Perinereis aibuhitensis., Natural Science Research, Faculty of Integrated Arts and Sciences, The University of Tokushima, Vol.21, 19-32, 2007. (Tokushima University Institutional Repository) ● Metadata: 117530 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1520009409319565824 (Tokushima University Institutional Repository: 117530, CiNii: 1520009409319565824)
2.	山中瑞江, 脇加奈子, 尾崎絵里香, 金井拓, 金井悠一郎, 中辻嵩, 谷川和代, 橋本美城子, 森由美子, 倉林陽子, 岸本慎哉, 水本浩太, Minoru Watanabe, Masaya Satoh, Kazuhiro W. Makabe, Makoto Ohashi and Toshio Gotoh : Comparative study on the primary structure of globin chains of the extracellular giant hemoglobin from the polychaet Perinereis aibuhitensis and Tylonrrhynchus heterochaetus, Natural Science Research, Faculty of Integrated Arts and Sciences, The University of Tokushima, Vol.19, 63-92, 2005. (Keyword) giant hemoglobin / annelid / polychaete / phylogenetic tree / supramolecule (Tokushima University Institutional Repository) ● Metadata: 117481 (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1520290882530406912 (Tokushima University Institutional Repository: 117481, CiNii: 1520290882530406912)
3.	Toshio Gotoh : Studies on erythrocruorin of Tylorrhynchus heterochaetus. V. Dissociation of 54,000 molecular weight subunit., Journal of Science of College of General Education, University of Tokushima, Vol.15, 1-10, 1982.
4.	Toshio Gotoh : Studies on erythrocruorin of Tylorrhynchus heterochaetus. III. Subunit composition of the erythrocruorin., Journal of Science of College of General Education, University of Tokushima, Vol.13, 1-7, 1980.
5.	Toshio Gotoh : Studies on erythrocruorin of Tylorrhynchus heterochaetus. IV. Separation of subunits associated with heme groups in situ., Journal of Science of College of General Education, University of Tokushima, Vol.12, 1-16, 1979.
6.	Toshio Gotoh and Y. Takeuchi : Studies on erythrocruorin of Tylorrhynchus heterochaetus. II. Identification of the polypeptide chain which is involved in heme binding., Journal of Science of College of General Education, University of Tokushima, Vol.10, 19-29, 1977.
7.	Toshio Gotoh : Studies on erythrocruorin of Tylorrhynchus heterochaetus. I. Isolation., Journal of Science of College of General Education, University of Tokushima, Vol.8, 1-15, 1975.
8.	Toshio Gotoh : Purification of human fibrin stabilizing factor., Journal of Science of College of General Education, University of Tokushima, Vol.6, 1-7, 1973.
9.	Toshio Gotoh : Proteolysis of fibrin stabilizing factor by thrombin., Science Report of Tohoku University Ser. IV (Biology), Vol.36, 61-74, 1971.
10.	Toshio Gotoh : Purification of bovine fibrin stabilizing factor., Science Report of Tohoku University Ser. IV (Biology), Vol.36, 57-60, 1971.

Review, Commentary:

1.	Toshio Gotoh : Oxygen-binding and related proteins: Structure, function and evolution, Comparative Physiology and Biochemistry, Vol.16, 233-236, Aug. 1999.
2.	蝦名恵 and Toshio Gotoh : ヘモグロビンの超分子生物学, KAGAKU, Vol.67, No.3, 226-232, Mar. 1997. (Link to Search Site for Scientific Articles) ● CiNii @ National Institute of Informatics (CRID): 1522543655161423872 (CiNii: 1522543655161423872)
3.	Toshio Gotoh : Structure and function of invertebrate haemoglobins, Comparative Physiology and Biochemistry, Vol.12, 418-421, Aug. 1995.
4.	Toshio Gotoh : ゴードン会議ー酸素結合タンパク質ーに参加して, Comparative Physiology and Biochemistry, Vol.11, 311-333, Aug. 1994.
5.	Toshio Gotoh : 環形動物巨大ヘモグロビンの分子構築, Seikagaku, Vol.61, 44-48, Feb. 1989.

Proceeding of International Conference:

1.	S Marco, J.C. Taveau, Toshio Gotoh, J.N. Lamy and J.J. Childress : Three-dimensional reconstruction of Tylorrhynchus heterochaetus hemoglobin, XIIth International Conference on Invertebrate O2 Binding Proteins, Roscoff, France, Jul. 2000.
2.	F. Zal, X. Bailly, Toshio Gotoh, F.H. Lalllier, A. Toulomnd and J.J. Childress : Free cystein residues:active sites for "new" functions in worm hemogoboins, sulfide carrying and/or trapping, XIIth International Conference on Invertebrate O2 Binding Proteins, Roscoff, France, Jul. 2000.
3.	F. Zal, Toshio Gotoh and A. Toulmond : The novel function of giant hemoglobins from tubeworms and annelids, Comparative Biochemistry and Physiology, Vol.124A (Suppl.), No.Supplement 1, S16, Calgary, Aug. 1999.
4.	Mariko Yamaki, Kiyohiro Imai, Kenji Kubota, Satoshi Ebina and Toshio Gotoh : A submultiple is a basic functional unit of annelid extracellular multisubunit hemoglobin identified by dynamic light scattering, transmission electronmicroscopy, circular dichroism, and oxygen binding property measurements, Comparative Biochemistry and Physiology, Vol.124A (Suppl.), No.Supplement 1, S95, Calgary, Aug. 1999.
5.	K. Matsubara, M. Yamaki, S. Ebina and Toshio Gotoh : Lectin-like binding activity of linker L2 in giant hemoglobin from Perinereis aibuhitensis, Comparative Biochemistry and Physiology, Vol.124A (Suppl.), No.Supplement 1, S94, Calgary, Aug. 1999.
6.	K. Matsubara, M. Yamaki, S. Ebina and Toshio Gotoh : Agglutinin-like activity of linker chains of giant hemoglobin from Perinereis aibuhitensis, Oxygen Binding and Oxygen Activating/Sensing Heme Proteins., Asilomar, Sep. 1998.
7.	Toshio Gotoh, T. Sano, A. Shibuya, M. Yamaki, M. Matsubara, K. Imai and S. Ebina : Reassembly of an annelid giant hemoglobin from Perinereis aibuhitensis, Oxygen Binding and Oxygen Activating/Sensing Heme Proteins., Asilomar, Sep. 1998.
8.	A. Shibuya, M. Yamaki, S. Ebina, K. Imai and Toshio Gotoh : Structural stability of the extracellular hemoglobin of Marphysa sanguinea, Oxygen Binding and Oxygen Activating/Sensing Heme Proteins., Asilomar, Sep. 1998.
9.	Toshio Gotoh, Matsubara Keiko, yamaki Mariko, Nagayama Kuniakai and Ebina Satoshi : Molecular basis of carbohydrate gluing in the supramolecular architecture of marine-worm giant hemoglobin., Pacifichem 1995, Symposium :"Invertebrate Hemoglobins", Hawaii, Dec. 1995.
10.	Toshio Gotoh, Matsubara Keiko., Yamaki Mariko, Nagayama N., Shibuya Akihiro and Ebina Satoshi : Disassembly and reassembly of the giant hemoglobin from thePerinereis aibuhitensis., Physiological Zoology, Vol.68, No.4, 217-226, Birmingham, Jul. 1995.
11.	Yamaki Mariko, Matsubara Keiko, Ebina Satoshi, Nagayama Kuniaki and Toshio Gotoh : Electron microscopic structural analysis of annelid giant hemoglobin., Gordon Research Conference, Plymouth, New Hampshire, Jul. 1994.
12.	Ebina Satoshi, Matsubara Keiko, Yamaki Mariko, Yamamoto M., Nagayama Kuniaki and Toshio Gotoh : Supermolecular architecture in large proteins as glued by carbohydrates., 1st East Asia Symposium of Biophysics, Himeji, Japan, May 1994.
13.	Imai K., Hori H. and Toshio Gotoh : Oxygen binding and spectroscopic properties of hemoglobin from the marine worm, Marphysa sanguinea Montagu., 3rd International Congress of Comparative Physiology and Biochemistry, Tokyo, Aug. 1991.
14.	Toshio Gotoh, Tomohiko Suzuki and Takashi Takagi : Structure of the extracellular hemoglobin of Tylorrhynchus heterochaetus., Structure and Function of Invertebrate Oxygen Carriers, 217-226, Whistler, Canada, Jul. 1990.
15.	Toshio Gotoh, Tomohiko Suzuki and Takashi Takagi : Nomenclature of the major constituent chains common to annelid extracellular hemoglobins., Structure and Function of Invertebrate Oxygen Carriers, 279-283, Whistler, Canada, Jul. 1990.
16.	Tomohiko Suzuki and Toshio Gotoh : Subunit structure and amino acid sequence of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus., Invertebrate Oxygen Carriers, 69-72, Tutzing, Jul. 1986.
17.	Fumio Shishikura, Toshio Gotoh, Walz A. Daniel, Snow June and Vinogrodov N. Serge : Primary structure of the monomer subunit of Lumbricus terrestris hemoglobin., --- Homology with other extracellular hemoglobin subunits ---, Biophysical Journal, Vol.49, No.2-2, 542a, San Francisco, Feb. 1986.

Proceeding of Domestic Conference:

1.	Norihiko Koori, Takahito Saito, Kazuhide Kanenishi, Tetsuya Yoshinaga, Ken'ichi Fujimoto, Toshio Gotoh and Seiichi Wakaizumi : eコンテンツ開発の現状とコース管理システムMoodle, 平成19年度全学FD 徳島大学教育カンファレンス発表抄録集, 44-45, Jan. 2008. (Summary) 大学教育委員会のeコンテンツ実用化WGは，オープンコースウェアの開発と大学内におけるICTを利用した教育改善を目指して，活動している．昨年来，高大接続教育，初年次教育にはeコンテンツが有用であろうと，徳大で要望のある高大接続のための物理と生物のeコンテンツを開発してきている．また，基礎物理学の自習・演習課題のeコンテンツも作成している．これらのeコンテンツは，オープンソースのコース管理システムMoodleの元に置かれて，学生への便宜を図っている．発表では，全体的な現状についてポスターで発表する． (Keyword) eコンテンツ
2.	Norihiko Koori, Takahito Saito, Makoto Ohashi, Seiichi Wakaizumi, Toshio Gotoh, Tetsuya Yoshinaga and Ken'ichi Fujimoto : 2006年問題に対するeコンテンツ開発と学習環境の整備, 平成18年度全学FD 徳島大学教育カンファレンス発表抄録集, 51-52, Mar. 2007. (Summary) 昨年度，大学教育委員会の下で「2006年問題検討WG」により，高校の新指導要領に基づく教育を受けた学生に対する高大接続の在り方，具体的対応策などが検討された．その中で指摘，提案された事項の内，本年度，「eコンテンツによる初年次学生の学習支援」のプロジェクトとして，インテリジェント・ラボにおいて高校での未履修科目のeコンテンツの開発，基礎科目の自習教材，それらを提供する学習環境(CMS)の整備などを行っているので，状況を報告する．
3.	Minoru Watanabe, 水本浩太, 山中瑞恵, Kazuhiro W. Makabe and Toshio Gotoh : アオゴカイ巨大ヘモグロビンのグロビンmRNAとその発現組織, 平成18年度生物系三学会中国四国支部大会，会報, 18, May 2006.
4.	水本浩太, 山中瑞江, Kazuhiro W. Makabe, Minoru Watanabe and Toshio Gotoh : アオゴカイ細胞外ヘモグロビンのグロビン鎖に含まれるCyc残基の位置とグロビン鎖の共通名, 第116回徳島生物学会会報, 15, Dec. 2005.
5.	Taku Kanai, Takanori Satoh and Toshio Gotoh : Reassociation of annelid giant hemoglobin from the polychaete Perinereis aibuhitensis, The 116th Annual Meeting of Tokushima Biological Society,Abstracts, Vol.58, No.2, 14, Dec. 2005.
6.	Toshio Gotoh, 尾崎絵理香, 野網明子, 金井拓, 水本浩太, Minoru Watanabe and Kazuhiro W. Makabe : アオゴカイPerinereis aibuhitensis巨大ヘモグロビンのアミノ酸配列, 平成17年度生物系三学会中国四国支部大会岡山大会，会報, 18, May 2005.
7.	Kanako Waki and Toshio Gotoh : Amino acid sequences of the constituent chains of giant hemoglobin from the polypeptide Perinereis aibuhitensis and phylogenetic tree of annelid hemoglobins, Comp. Biochem. Physiol., Vol.134A, No.1, 223, Jan. 2003.
8.	脇加奈子, 落合威彦 and Toshio Gotoh : 環形動物巨大ヘモグロビンの質量分析と分子系統樹, 徳島生物学会第106 回大会, Dec. 2002.
9.	Toshio Gotoh, 脇加奈子 and 今井清博 : 環形動物巨大ヘモグロビンの構造, Comparative Physiology and Biochemistry, Vol.74, No.8, 96, Oct. 2002.
10.	Toshio Gotoh : 環形動物巨大ヘモグロビンの構造, 第75回日本生化学会大会，シンポジュウム;酸素トランスポーターの多様性と機能進化, Oct. 2002.
11.	谷川和代, 橋本美城子, Brian N. Green and Toshio Gotoh : アオゴカイ巨大ヘモグロビン，グロビン鎖のアミノ酸配列, 日本動物学会中国四国支部会大会, May 2002.
12.	Toshio Gotoh, 四方田千佳子, 中西優子 and 脇加奈子 : 環形動物巨大ヘモグロビンのグロビン 12 量体, 日本動物学会中国四国支部大会, May 2001.
13.	Toshio Gotoh, 森由美子, 倉林陽子· and 村上聡 : アオゴカイ Perinereis aibuhitensis 巨大ヘモグロビンの部分構造, 日本動物学会中国四国支部大会, May 2000.
14.	Toshio Gotoh : 巨大ヘモグロビンをオーガナイズするリンカーの結合様式と分子進化, 日本生物物理学会，シンポジューム:ヘモグロビン研究の意外な展開: グロビン分子進化研究の最前線, Nov. 1996.
15.	Toshio Gotoh : 巨大ヘモグロビンをつなぐリンカー糖鎖分子, 蛋白研セミナー; 蛋白質とフロンテイアバイオロジー:構造と分子進化の視点から, Mar. 1996.
16.	Toshio Gotoh : 環形動物細胞外ヘモグロビン巨大化の分子機構, 自然科学研究機構，分子科学研究所;分子研セミナー;, Dec. 1994.
17.	Toshio Gotoh : Thrombin による Fibrin Stabilizing Factor の活性化, 酵素科学シンポジュウム予稿集, Vol.12, 346-348, Aug. 1966.

Professor Emeritus : Gotoh, Toshio

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