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.
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
MLA
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
HARVARD
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
VANCOUVER
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
)
View on SCiNiTO