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- W2019965724 abstract "1.|Thrombin (EC 3.4.4.13), plasmin (EC 3.4.4.14) and trypsin (EC 3.4.4.4) were examined with regard to their differential specificities toward arginyl and lysyl compounds. 2.|A series of eight arginyl and lysyl peptides were synthesized and, together with an arginyl and lysyl ester, were compared as substrates and inhibitors of these enzymes. The compounds include Na-tosyl-l-arginylglycine and its methyl ester, Na-tosyl-l-arginylsarcosine and its methyl ester, the lysine analogues of these peptides, and the methyl esters of Na-tosylarginine and Na-tosyllysine. 3.|Both carboxy- and amino-terminal analyses were performed on fibrin digested by plasmin and trypsin and the bonds broken compared. 4.|The results of these studies were consistent with the notion that thrombin has a high degree of specificity for the arginyl side chain and plasmin a preference for lysyl residues. Trypsin did not display a significant preference, hydrolyzing arginyl and lysyl bonds equally well." @default.
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- W2019965724 title "Differential specificities of thrombin, plasmin and trypsin with regard to synthetic and natural substrates and inhibitors" @default.
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- W2019965724 doi "https://doi.org/10.1016/0005-2744(72)90250-1" @default.
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