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- W63316641 abstract "Publisher Summary This chapter discusses the structural aspects of thrombin and prothrombin. The side-chain specificity of thrombin is similar to that of trypsin as shown by its preference for arginyl and lysyl esters and amides with a blocked α-amino group. However, the action of thrombin on polypeptide and protein substrates is much more limited and specific than that of trypsin and plasmin. In fibrinogen, which is its natural substrate, thrombin splits only four, or eventually six, out of 200–300 peptide bonds that are potential points of tryptic cleavage. Those four peptide bonds that are split by thrombin during normal clotting are Arg-Gly bonds, one in each of the two α ( A ) and the two β(B) chains of the fibrinogen molecule. Apart from fibrinogen, only two polypeptide substrates of known structure have been studied, namely, secretin and cholecystokinin-pancreozymin. In each case one single arginyl bond is split by thrombin." @default.
- W63316641 created "2016-06-24" @default.
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- W63316641 date "1970-01-01" @default.
- W63316641 modified "2023-09-27" @default.
- W63316641 title "Structural Aspects of Thrombin and Prothrombin" @default.
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- W63316641 doi "https://doi.org/10.1016/b978-0-12-211850-0.50015-x" @default.
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