BIOMAT Database Logo BIOMAT Database Logo

Characterization of the B-chain of human plasma alpha 2HS-glycoprotein. The complete amino acid sequence and primary structure of its heteroglycan. 1983

F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart

alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains. In the present study, we have separated these two chains from one another and have elucidated the complete primary structure of the B-chain. Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues. The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues. Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6). The structure of the B-chain was found to be as follows. (formula; see text) Thus, the molecular weight of the B-chain is 3386. Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol. 47, 45-148) predicts that the B-chain has two beta-turns. Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein. The second beta-turn probably includes the Cys residue which links the B- to the A-chain. In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.

UI MeSH Term Description Entries
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D001798 Blood Proteins Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins. Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D002240 Carbohydrate Sequence The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS. Carbohydrate Sequences,Sequence, Carbohydrate,Sequences, Carbohydrate
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular
D060749 alpha-2-HS-Glycoprotein A fetuin subtype that is synthesized by HEPATOCYTES and secreted into the circulation. It plays a major role in preventing CALCIUM precipitation in the BLOOD. alpha2 Heremans-Schmid Glycoprotein,AHSG Protein,Fetuin-A,alpha(2) HS Glycoprotein,alpha-2HS Glycoprotein,alpha2HS Glycoprotein,Fetuin A,alpha 2 HS Glycoprotein,alpha 2HS Glycoprotein

Related Publications

F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
The complete amino acid sequence of the A-chain of human plasma alpha 2HS-glycoprotein.
February 1986, The Journal of biological chemistry,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens.
February 1988, Proceedings of the National Academy of Sciences of the United States of America,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Solid-phase synthesis of the B-chain of human alpha 2HS glycoprotein.
July 1998, Carbohydrate research,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Purification and characterization of the two forms of human plasma alpha 2HS-glycoprotein.
November 1981, Biochimica et biophysica acta,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Complete amino acid sequence of human plasma beta 2-glycoprotein I.
June 1984, Proceedings of the National Academy of Sciences of the United States of America,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
The complete cDNA and amino acid sequence of bovine fetuin. Its homology with alpha 2HS glycoprotein and relation to other members of the cystatin superfamily.
March 1990, The Journal of biological chemistry,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Primary structure of human erythrocyte glycophorin A. Isolation and characterization of peptides and complete amino acid sequence.
October 1978, Biochemistry,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Human plasma alpha 1-acid glycoprotein--biochemical properties, the amino acid sequence and the structure of the carbohydrate moiety, variants and polymorphism.
January 1989, Progress in clinical and biological research,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence.
November 1979, Biochemistry,
F Gejyo, and J L Chang, and W Bürgi, and K Schmid, and G D Offner, and R F Troxler, and H Van Halbeek, and L Dorland, and G J Gerwig, and J F Vliegenthart
Single-chain structure of human ceruloplasmin: the complete amino acid sequence of the whole molecule.
January 1984, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!