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Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Purification and characterization of the carboxypeptidase
The Journal of Biological Chemistry
Jan 10, 1976
J F SeberWilliam M Awad
PMID: 399
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Abstract
We described earlier the facilitated purifications of the trypsin and aminopeptidase components present in Pronase (Vosbeck, K. D., Chow, K. -F., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 6029-6034). A partially resolved protein mixture left over after one of the steps in that pro...read more
Mentioned in this Paper
CPA1 gene
Enzymes, antithrombotic
Meniscus structure of joint
Enzymes, peripheral vasodilators
Cations
Homologous Gene
Carboxypeptidase Activity
Pancreatic Carboxypeptidase A Activity
Serine Endopeptidases
Enzymes, hematological
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Proteolytic enzymes of the K-1 strain of Streptomyces griseus obtained from a commercial preparation (Pronase). Purification and characterization of the carboxypeptidase
Abstract
We described earlier the facilitated purifications of the trypsin and aminopeptidase components present in Pronase (Vosbeck, K. D., Chow, K. -F., and Awad, W. M., Jr. (1973) J. Biol. Chem. 248, 6029-6034). A partially resolved protein mixture left over after one of the steps in that pro...read more
Mentioned in this Paper
CPA1 gene
Enzymes, antithrombotic
Meniscus structure of joint
Enzymes, peripheral vasodilators
Cations
Related Papers
Paper Details
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