- 作者: 張曙明
- 作者服務機構: Institute of Chemistry; Academia Sinica
- 中文摘要: 1. The extracellular enzymes secreted by Actinomucor elegans were investigated on their proteolytic activites which were assayed by the Kunitz method with casein as the substrate.2. The extracellular enzyme solution was partially purified by fractionation with ammonium sulfate. It was noted that there were at least three enzyme systems of different pH optimums.3. The stability of each of these three enzyme systems could be discriminated by incubation at 28-29°C for 21 hours. The enzyme system at pH 7.5 was found stable at pH 8.0; whereas that at pH 8.4 stable at pH 9.0 and that at pH 10.5 stable at pH 10.0.4. The rate of hydrolysis of casein by the enzyme solution was proportional to the temperature. The maximum activity was at 50-60°.5. The enzyme solution was quite active against a casein substrate and much less active against hemoglobin, edestin, ovalbumin and soybean albumin.6. The enzyme was active against some synthetic substrates such as N-benzoyl-L- arginine ethyl ester and N-benzoyl-L-arginine amide for trypsin and L-tyrosine ethyl ester for chymotrypsin but no hydrolysis was observed on denatured hemo- globin at pH 1.8 for pepsin.7. The enzyme was inhibited by the extract of potato, EDTA and some divalent ions, such as , and , and somehow activated by sodium chloried, cysteine and .
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