作者: Sam Seifter , Elvin Harper
DOI: 10.1016/S1874-6047(08)60409-6
关键词: Clostridium histolyticum 、 Substrate (chemistry) 、 Cysteine 、 Collagen helix 、 Peptide bond 、 Enzyme 、 Biochemistry 、 Synovial fluid 、 Chemistry 、 Collagenase
摘要: Publisher Summary This chapter describes the collagenases of Clostridium histolyticum , collagenase tadpole Rana catesbiana and human rheumatoid synovial fluid. A is defined as an enzyme capable causing hydrolytic scission peptide bonds located in characteristic poly-L-proline type helical regions when substrate undenatured state. Almost all are inhibited by ethylenediaminetetraacetate (EDTA) these except that Trichophyton schoenleinii appear to require Ca 2+ for activity. Several cysteine, and, these, a group appears contain zinc or some other metal their structures. However, there both bacterial tissue not be cysteine. The laboratory applications have been limited largely clostridiopeptidase A. Clostridial employed study crystalline collagen molecule also provide fragments from amorphous regions. Clostridiopeptidase has used effectively unfolding refolding helix.