Structure of the carboxyl-terminal half of human a...[J Biochem. 1986]

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1: J Biochem. 1986 Nov;100(5):1399-402. Links

Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor deduced from that of cDNA.

Sumi Y, Nakamura Y, Aoki N, Sakai M, Muramatsu M.

A 1.7 kilobase cDNA clone isolated from a human liver cDNA library contained 822 nucleotides encoding the carboxyl-terminal 274 amino acid sequence of alpha 2-plasmin inhibitor, a stop codon and a 3' noncoding region of 0.9 kilobases. The amino acid sequence deduced from the cDNA shows 29-31% homology with those of other plasma protease inhibitors. The inhibitor's putative reactive-site peptide bond was Met-Ser, and the Met residue was located at the 91st position from the carboxyl-terminal end. The plasminogen binding site was located in the carboxyl-terminal region.

PMID: 3818581 [PubMed - indexed for MEDLINE]

Structure of human alpha 2-plasmin inhibitor deduced from the cDNA sequence. [J Biochem. 1987]
Primary structure of human alpha 2-antiplasmin, a serine protease inhibitor (serpin). [J Biol Chem. 1987]
Organization of the human alpha 2-plasmin inhibitor gene. [Proc Natl Acad Sci U S A. 1988]
ReviewMolecular genetics of alpha 2 plasmin inhibitor. [Adv Exp Med Biol. 1990]
ReviewGenomic organization of the human alpha 2-plasmin inhibitor. [Nippon Ketsueki Gakkai Zasshi. 1988]

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Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor deduced from that of cDNA.

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