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Some Properties of Alkaline Protease in Rat Muscle Compared with That in Peritoneal Cavity Cells
- Source :
- Agricultural and Biological Chemistry. 40:927-933
- Publication Year :
- 1976
- Publisher :
- Oxford University Press (OUP), 1976.
-
Abstract
- Further studies were made on muscle alkaline protease and, at the same time, its properties were compared with those of the protease in peritoneal cavity cells. Both enzymes showed similar properties. Their molecular weight was 22,000, optimum temperature 57°C, optimum pH 9.0~10.5. They were slightly inhibited by soybean trypsin inhibitor. Tosylphenylalaninechloromethylketone inhibited both enzymes but tosyllysinechloromethylketone did not. Both enzymes cleaved peptide bonds Tyr (16)-Leu(17), Phe(24)-Phe(25) of oxidized B chain of insulin.
- Subjects :
- chemistry.chemical_classification
Protease
Kunitz STI protease inhibitor
Chemistry
medicine.medical_treatment
Insulin
Alkaline protease
Molecular biology
General Biochemistry, Genetics and Molecular Biology
Peritoneal cavity
medicine.anatomical_structure
Enzyme
Biochemistry
medicine
Peptide bond
General Agricultural and Biological Sciences
Subjects
Details
- ISSN :
- 00021369
- Volume :
- 40
- Database :
- OpenAIRE
- Journal :
- Agricultural and Biological Chemistry
- Accession number :
- edsair.doi.dedup.....bede7ebf916239b54496d4f3eee56d63