The Covalent Differences between Bovine (Y- and j?-Thrombin

نویسندگان

  • Roger L. Lundblad
  • Claudia M. Noyes
  • Kenneth G. Mann
  • Henry S. Kingdon
چکیده

The partial covalent structure of bovine /I-thrombin has been determined by the use of automated Edman degradation and carboxypeptidase digestion of the component polypeptide chains separated by gel filtration following either reduction and carboxymethylation or performic acid oxidation. /I-Thrombin has been found to contain three peptide chains derived by proteolysis of the parent a-thrombin molecule. The A chain of a-thrombin has been cleaved at two points yielding a peptide (Al chain) which contains 17 amino acids, beginning with threonine 14 and ending with lysine 30. The B chain of a-thrombin has been cleaved at two positions to yield a Bl chain which begins with the NHz-terminal isoleucine and terminates with lysine 65 and a B2 chain which begins with lysine 74 and continues through COOH-terminal serine 259. The Al chain and B2 chain are linked by a disulfide bridge. Although there is no evidence for a covalent bond between the Bl chain and the B2-Al chains, the Bl chain is tightly bound to the remainder of the molecule, for separation is achieved only under denaturing conditions.

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تاریخ انتشار 2002