Exciton chirality method and its application to configurational and conformational studies of natural products
摘要:
1. 1. Proteinase activity is evidenced in coelomic cell lysate of Eisenia fetida andrei.2. 2. Tested on gelatin plates, the proteolysis develops rapidly during the first hr of incubation at 37°C.3. 3. The proteolysis is pH-dependent with two optima for pH 7.0 and 10.0.4. 4. The proteolysis is dose-dependent.5. 5. The proteolysis is not influenced by ionic strength.6. 6. The proteolysis is thermo-sensitive but not totally suppressed by 15 min at 100°C.7. 7. Three serine proteases, A2 (Mr 42 kDa), B2 (Mr 46 kDa) and C2 (Mr 48 kDa), were purified by affinity chromatography on benzamidine-Sepharose.8. 8. According to various inhibition and activity tests, A2 is of trypsin-like type, Ca2+-independent but Mg2+- and Mn2+-dependent and C2 is of chymotrypsin-like type.
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DOI:
10.1021/ar50056a001
被引量:
年份:
1972
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