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Structure of the carboxyl-terminal half of human alpha 2-plasmin inhibitor deduced from that of cDNA.
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]
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Cited by 3 PubMed Central articles
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Organization of the human alpha 2-plasmin inhibitor gene.
Hirosawa S, Nakamura Y, Miura O, Sumi Y, Aoki N.
Proc Natl Acad Sci U S A. 1988 Sep; 85(18):6836-40.
[Proc Natl Acad Sci U S A. 1988]
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Interaction between plasminogen activator inhibitor type 1 (PAI-1) bound to fibrin and either tissue-type plasminogen activator (t-PA) or urokinase-type plasminogen activator (u-PA). Binding of t-PA/PAI-1 complexes to fibrin mediated by both the finger and the kringle-2 domain of t-PA.
Wagner OF, de Vries C, Hohmann C, Veerman H, Pannekoek H.
J Clin Invest. 1989 Aug; 84(2):647-55.
[J Clin Invest. 1989]
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Molecular basis for congenital deficiency of alpha 2-plasmin inhibitor. A frameshift mutation leading to elongation of the deduced amino acid sequence.
Miura O, Hirosawa S, Kato A, Aoki N.
J Clin Invest. 1989 May; 83(5):1598-604.
[J Clin Invest. 1989]