Carboxypeptidase N from Pig Serum
- 1 January 1976
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 357 (1), 867-872
- https://doi.org/10.1515/bchm2.1976.357.1.867
Abstract
Carboxypeptidase N [EC 3.4.12.7] was purified 865-fold from pig serum. The enzyme has a MW of .apprx. 315,000. In the presence of dodecylsulfate and mercaptoethanol, it dissociates into 3 subunits of MW = 90,000, 50,000, 30,000, respectively. The native enzyme and the subunit of MW = 90,000 contain carbohydrate; no carbohydrate is found in the subunits of MW = 50,000 and 30,000. Trypsin [EC 3.4.21.4] transforms carboxypeptidase N into a form having a smaller molecular weight and enhanced activity.This publication has 12 references indexed in Scilit:
- Plasma carboxypeptidase N, subunits and characteristicsArchives of Biochemistry and Biophysics, 1975
- Column chromatography of amino acids with fluorescence detectionJournal of Chromatography A, 1973
- Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidaseJCI Insight, 1970
- Degradation of Human Fibrinopeptides A and B in Blood Serum in vitro.Acta Chemica Scandinavica, 1968
- Carboxypeptidase in blood and other fluids. Values in human blood in normal and pathological conditionsClinica Chimica Acta; International Journal of Clinical Chemistry, 1965
- An enzyme in human blood plasma that inactivates bradykinin and kallidinsBiochemical Pharmacology, 1962
- Influence of cobalt and cadmium on the peptidase and esterase activities of carboxypeptidase BBiochimica et Biophysica Acta, 1961
- CARBOXYPEPTIDASE-B .4. PURIFICATION AND CHARACTERIZATION OF THE PORCINE ENZYME1960
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951