Purification and properties of a peptidase acting on a synthetic substrate for collagenase from monkey kidney
| Autor: | S. Aswanikumar, A.N. Radhakrishnan |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Male
Cations Divalent medicine.medical_treatment Metal ions in aqueous solution Kinetics Biology Kidney Endopeptidases medicine Animals Edetic Acid chemistry.chemical_classification Oligopeptide Protease Substrate (chemistry) Dipeptides Mercury General Medicine Molecular biology Enzyme assay Molecular Weight Microbial Collagenase Enzyme chemistry Biochemistry Ethylmaleimide Collagenase biology.protein Hydroxymercuribenzoates Macaca Female Peptides Oligopeptides medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 384:194-202 |
| ISSN: | 0005-2744 |
| DOI: | 10.1016/0005-2744(75)90108-4 |
| Popis: | A peptidase cleaving a synthetic substrate for collagenase, 4-phenylazobenzyloxycarbonyl-L-Pro-L-Leu-Gly-L-Pro-D-Arg (designated as PZ-peptide) has been purified extensively (about 5200-fold) from a soluble extract of monkey kidney with a view of carrying out studies on its possible physiological role. The purified PZ-peptidase appeared essentially free of collagenase, nonspecific protease and di- and tri-peptidase activities. The properties of the purified PZ-peptidase resemble very much the granuloma enzyme. It is optimally active around pH 7.0. Its apparent Km value for PZ-peptide is 0.72 mM and V is 10.1 mumol/mg protein/min. It is reversibly inhibited by p-hydroxymercuribenzoate and HgCl2, whereas iodoactetamide does not affect the enzyme activity. N-Ethylmaleimide inhibited the enzyme partially (50%). Heavy metals like Cu-2+, Cd-2+, Ag+, Pb-2+, Ni-2+, and Zn-2+ completely inhibited the enzyme activity, while the inhibition by Co-2+ was only partial. Fe-2+ did not exert any effect on the activity. The enzyme activity was completely inhibited by EDTA and was restored almost to the original value by metal ions like Mn-2+, Mg-2+, Ca-2+ and Ba-2+. The approximate molecular weight of the purified enzyme was estimated to be 56 000. |
| Databáze: | OpenAIRE |
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