Effect of pH and Sodium Chloride on Activation of Prorennin
Open Access
- 1 November 1964
- journal article
- research article
- Published by American Dairy Science Association in Journal of Dairy Science
- Vol. 47 (11) , 1181-1187
- https://doi.org/10.3168/jds.s0022-0302(64)88878-0
Abstract
Prorennin was extracted from calf-stomach tissue and purified by a modification of Foltmann''s procedure. Both pH and NaCl concentration were shown to have considerable effect on the rate of activation of prorennin as well as the final yield of activity. Greatest yields of stable activity were obtained by activating at pH 5.0 in the presence of 1.5 - 2.0 [image] NaCl. At lower pH values activation was more rapid, but the activated enzyme was less stable. Activation at pH 2.0 - 4.0 was extremely rapid and gave high yields of activity which quickly deteriorated. Also the presence of any amount of NaCl in that pH range inhibited activation and reduced yields; the greater the salt concentration, the greater the effect. The activation of prorennin at pH 5.0 and 4.7 was predominantly autocatalytic, but there was evidence of a limited non-autocatalytic activation that occurred before autocatalysis became predominant. Activation at pH 2.0 was very rapid, even at low temperatures, and the kinetics under these conditions could not be followed with any degree of accuracy.Keywords
This publication has 14 references indexed in Scilit:
- Studies on Rennin. V. Chromatographic Purification of Prorennin.Acta Chemica Scandinavica, 1960
- Studies on Rennin. II. On the Crystallisation, Stability and Proteolytic Activity of Rennin.Acta Chemica Scandinavica, 1959
- Heterogeneity of Crystalline RenninJournal of Dairy Science, 1958
- On the Purification of Prorennin with a Note on the Recrystallization of Rennin.Acta Chemica Scandinavica, 1958
- The preparation of crystalline rennin and a study of some of its propertiesArchives of Biochemistry and Biophysics, 1953
- Some observations on the determination of the activity of rennetThe Analyst, 1952
- The purification and crystallization of renninBiochemical Journal, 1945
- ISOLATION, CRYSTALLIZATION, AND PROPERTIES OF SWINE PEPSINOGENThe Journal of general physiology, 1938
- ISOLATION FROM BEEF PANCREAS OF CRYSTALLINE TRYPSINOGEN, TRYPSIN, A TRYPSIN INHIBITOR, AND AN INHIBITOR-TRYPSIN COMPOUNDThe Journal of general physiology, 1936
- Über das Labzymogen des Kalbsmagens.Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1911