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- W2068808542 abstract "Moojeni protease A, a proteolytic enzyme isolated from Bothrops moojeni venom, hydrolyzes type I collagen, gelatin, fibrinogen, fibrin and the B-chain of oxidized insulin. The proteinase cleaves the Aα-chain faster than the Bβ-chain of human fibrinogen and shows no effect on the γ-chain. Fibrin solubilization appears to occur from the hydrolysis of the α-polymer and unpolymerized α-chain. The enzyme cleaves the Ala(14)-Leu(15) bond of the oxidized insulin B-chain most rapidly, followed by splitting the Ser(9)-His(10) bond. The Tyr(16)-Leu(17) and Gly(20)-Glu(21) cleavage sites were hydrolyzed slightly more slowly, while the peptide bonds His(5)-Leu(6), His(10)-Leu(11), Glu(21)-Arg(22), Gly(23)-Phe(24) and Phe(24)-Phe(25) were more resistant to the enzyme attack. Small synthetic peptides were not hydrolyzed by moojeni protease A." @default.
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- W2068808542 date "1993-02-01" @default.
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- W2068808542 title "Proteolytic specificity of moojeni protease A isolated from the venom of Bothrops moojeni" @default.
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- W2068808542 doi "https://doi.org/10.1016/0041-0101(93)90285-q" @default.
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