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en: Novel S-S loops in the globin chains from the giant hemoglobin of the polychaete Perinereis aibuhitensis.

en: Natural Science Research

ja: Natural Science Research


en: Domain-domain interactions of HtpG, an Escherichia coli homologue of eukaryotic HSP90 molecular chaperone

en: 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.

en: European Journal of Biochemistry

ja: European Journal of Biochemistry


en: Electrospray Ionization Mass Spectrometric Observation of Large, Noncovalent Globin Subassemblies in the ~3600 kDa Hexagonal Bilayer Hemoglobins

en: Journal of Molecular Biology

ja: Journal of Molecular Biology


en: Heavy-metal induced changes in cellular nonproteinaceous thiol levels and heavy metal-binding peptides in Tetraselmis tetrathele (Prasinophyceae)

en: 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.

en: Journal of Phycology

ja: Journal of Phycology


en: Carbohydrate-gluing is a strategy for supramolecular clamping of submutiples in annelid extracellular multi-subunit hemoglobin

en: 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.

en: Archives of Biochemistry and Biophysics

ja: Archives of Biochemistry and Biophysics


en: Hexagonal bilayer structuring activity of linker chains of an annelid giant hemoglobin from the polychaete Perinereis aibuhitensis


en: Wheat germ agglutinin-reactive chains of giant hemoglobin from the polychaete Perinereis aibuhitensis.

en: 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.

en: Biochimica et Biophysica Acta (BBA) - General Subjects


en: Identification of the subunit loci in the extracellular multisubunit hemoglobin from annelid Perinereis aibuhitensis.


en: Electrospray ionization mass spectrometric determination of the complete polypeptide chain composition of Tylorrhynchus heterochaetus hemoglobin.

en: The Journal of Biological Chemistry

ja: The Journal of Biological Chemistry


en: Carbohydrate gluing, an architectural mechanism in the supramolecular structure of an annelid gaint hemoglobin.

en: Proceedings of the National Academy of Sciences of the United States of America


en: Primary structure of two linker chains of the extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.


en: Molecular assembly and evolution of multi-subunit extracxellular annelid hemoglobins.

en: Zoological Science

ja: Zoological Science


en: Spectrophotometric, electron paramagnetic resonance and oxygen binding studies on the hemoglobin from the marine polychaete Perinereis aibuhitensis (Grube): comparative physiology of hemoglobin.

en: The Journal of Biochemistry

ja: The Journal of Biochemistry


en: Immunological relatedness of annelid extracellular hemoglobins and chlorocruorins.

en: Comparative Biochemistry and Physiology

ja: Comparative Biochemistry and Physiology


en: Small-angle X-ray scattering studies of annelid giant haemoglobin from Tylorrhynchus heterochaetus

en: Int. J. Biol. Macromol.

ja: Int. J. Biol. Macromol.


en: An evolutionary tree for invertebrate globin sequences.

en: Journal of Molecular Evolution

ja: Journal of Molecular Evolution


en: Novel S-S loops in the giant hemoglobin of Tylorrhynchus heterochaetus.


en: The calcium, copper and zinc content of some annelid extracellular haemoglobins.

en: The Biochemical Journal

ja: The Biochemical Journal


en: Amino acid sequence of the monomer subunit of the extracellular hemoglobin of Lumbricus terrestris.

en: The Journal of Biological Chemistry


en: Two globin strains in the giant annelid extracellular haemoglobins.


en: Subunit assembly of giant haemoglobin from the polychaete Tylorrhynchus heterochaetus.

en: Journal of Molecular Biology


en: Preparation and characterization of monoclonal antibodies to the extracellular hemoglobin of Lumbricus terrestris.

en: 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.

en: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology


en: Amino acid sequence of the smallest polypeptide chain containing heme of extra-cellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.

ja: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology


en: The complete amino acid sequence of giant multisubunit hemoglobin from the polychaete Tylorrhynchus heterochaetus.


en: Isolation of the subunits and polypeptide chains of the extracellular hemoglobin of Lumbricus terrestris.

en: Biophysical Journal

ja: Biophysical Journal


en: Amino ascid sequence of polypeptide chain IIB of extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus.


en: Subunit structure of extracellular hemoglobin from the polychaete Tylorrhynchus heterochaetus and amino acid sequence of the constituent polypeptide chain (IIC).


en: Auto-deoxygenation of annelid giant haemoglobin in vitro.

en: Int. J. Biol. Macromol.


en: Autoxidation of extracellular oxyhaemoglobin from the polychaete Perinereis brevicirris (Grube).

en: Comparative Biochemistry and Physiology


en: Separation of constituent polypeptide chains containing heme from extracellular hemoglobin of the polychaete Perinereis brevicirris (Grube).


en: Subunit structure of erythrocruorin from the polychaete Tylorrhynchus heterochaetus.

en: The Journal of Biochemistry


en: Generation of superoxide radical during the autoxidation of oxymyoglobin.


en: Autoxidation of native oxymyoglobin from bovine heart muscle.

en: Archives of Biochemistry and Biophysics


en: Effect of intracellular organic phosphate on the oxygen equilibrium curve of chicken hemoglobin.


en: Chromatographic separation of oxy- and met-myoglobin on a DEAE-cellulose column.

en: Journal of Chromatography. A.

ja: Journal of Chromatography. A.


en: Fibrinoligase: The fibrin stabilizing factor system.

en: Methods in Enzymology

ja: Methods in Enzymology


en: The transpeptidase system which crosslinks fibrin by γ-glutamyl-ε-lysine bonds.

en: Biochemical and Biophysical Research Communications


en: Reassociation of annelid giant hemoglobin from the polychaete Perinereis aibuhitensis.

en: Natural Science Research, Faculty of Integrated Arts and Sciences, The University of Tokushima

ja: 徳島大学総合科学部自然科学研究


en: Comparative study on the primary structure of globin chains of the extracellular giant hemoglobin from the polychaet Perinereis aibuhitensis and Tylonrrhynchus heterochaetus

ja: 徳島大学総合科学部自然科学研究


en: Studies on erythrocruorin of Tylorrhynchus heterochaetus. V. Dissociation of 54,000 molecular weight subunit.

en: Journal of Science of College of General Education, University of Tokushima


en: Studies on erythrocruorin of Tylorrhynchus heterochaetus. III. Subunit composition of the erythrocruorin.

ja: Journal of Science of College of General Education, University of Tokushima


en: Studies on erythrocruorin of Tylorrhynchus heterochaetus. IV. Separation of subunits associated with heme groups in situ.


en: Studies on erythrocruorin of Tylorrhynchus heterochaetus. II. Identification of the polypeptide chain which is involved in heme binding.


en: Studies on erythrocruorin of Tylorrhynchus heterochaetus. I. Isolation.


en: Purification of human fibrin stabilizing factor.


en: Proteolysis of fibrin stabilizing factor by thrombin.

en: Science Report of Tohoku University Ser. IV (Biology)


en: Purification of bovine fibrin stabilizing factor.

ja: Science Report of Tohoku University Ser. IV (Biology)