AI-Kadeeb,, S. (2005). PARTIAL PURIFICATION AND PROPERTIES OF L- ALANINE DEHYDROGENASE OF Aspergillus terreus. Journal of Plant Production, 30(9), 5159-5168. doi: 10.21608/jpp.2005.237468
Siham A. AI-Kadeeb,. "PARTIAL PURIFICATION AND PROPERTIES OF L- ALANINE DEHYDROGENASE OF Aspergillus terreus". Journal of Plant Production, 30, 9, 2005, 5159-5168. doi: 10.21608/jpp.2005.237468
AI-Kadeeb,, S. (2005). 'PARTIAL PURIFICATION AND PROPERTIES OF L- ALANINE DEHYDROGENASE OF Aspergillus terreus', Journal of Plant Production, 30(9), pp. 5159-5168. doi: 10.21608/jpp.2005.237468
AI-Kadeeb,, S. PARTIAL PURIFICATION AND PROPERTIES OF L- ALANINE DEHYDROGENASE OF Aspergillus terreus. Journal of Plant Production, 2005; 30(9): 5159-5168. doi: 10.21608/jpp.2005.237468
PARTIAL PURIFICATION AND PROPERTIES OF L- ALANINE DEHYDROGENASE OF Aspergillus terreus
Botany Department, Girls College of Education in Riyadh, Kingdom of Saudia Arabia
Abstract
L-Alanine dehydrogenase was partially purified about 13-lold in a two-step purification from the cell free extracts of Aspergillus tettcvs. Maximal enzyme activity occurred at pH 8.6 for reductive arnlnatlon of pyruvate, where pH 10.4 for oxidative deamination of L-alanine and at a temperature of 25°C. The Km values for pyruvate. NH:, NADH, L-alanine and NAD' were 4, 175.4, 0.526, 16.13 and 3.3 mM respectively. The enzyme activity was activeted by CO",Fe", ln2' , Ca". and Cu2'. SH groups don't seem to playa role in the catalytic action of the enzyme as addition of roooacetate or dithiothreitol did not effected the enzyme activity. Stability of the enzyme under different conditions was investigated.