| Literature DB >> 1576209 |
M P Papet1, D Delay, M Monsigny, F Delmotte.
Abstract
Alpha- and beta-D-galactosidases were characterized from a hydroalcoholic extract of wheat germ (Triticum vulgare). Kinetic constants (Vmax and KM) and the optimal pHs for the hydrolysis of p-nitrophenyl galactopyranosides by both enzymes were determined. These enzymes presented a high stability in hydroalcoholic medium and were inhibited by iodoacetamide and sodium p-hydroxy-mercuribenzoate.Entities:
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Year: 1992 PMID： 1576209 DOI： 10.1016/0300-9084(92)90183-f
Source DB: PubMed Journal: Biochimie ISSN： 0300-9084 Impact factor: 4.079