A specific alkaline phosphatase from Saccharomyces cerevisiae with protein phosphatase activity
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چکیده
منابع مشابه
Purification and Properties of Alkaline Phosphatase with Protein Phosphatase Activity from Saccharomyces cerevisiae
An alkaline phosphatase (A LPase) from Saccharomyces cerevisiae strain 257 was purified 345-fold with specific activity of 54 533 nmol x min“ 1 x mg protein-1 . It was shown to be a dimeric protein (apparent mol. wt. approx. 130 kDa) with optimum activity at pH 8.6 8.8 and good stability at 50 °C. The A LPase was a non-specific enzyme hydrolyzing a wide vari ety of monophosphate esters. The en...
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A phosphatase, active towards phosphorylase a and phosphorylated proteins casein and histone II-A, was isolated from Saccharomyces cerevisiae 257. The enzyme dephosphorylated glycogen phosphorylase from commercial yeast rendering it inactive. The protein phosphatase activity was not influenced by any metal ions. Phosphorylase phosphatase activity was slightly stimulated by p-nitrophenyl phospha...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1998
ISSN: 0378-1097
DOI: 10.1016/s0378-1097(98)00065-2