A specific alkaline phosphatase fromSaccharomyces cerevisiaewith protein phosphatase activity
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منابع مشابه
Phosphotyrosyl-specific protein phosphatase activity of a bovine skeletal acid phosphatase isoenzyme. Comparison with the phosphotyrosyl protein phosphatase activity of skeletal alkaline phosphatase.
A partially purified bovine cortical bone acid phosphatase, which shared similar characteristics with a class of acid phosphatase known as tartrate-resistant acid phosphatase, was found to dephosphorylate phosphotyrosine and phosphotyrosyl proteins, with little activity toward other phosphoamino acids or phosphoseryl histones. The pH optimum was about 5.5 with p-nitrophenyl phosphate as substra...
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Background: The present study was carried out on the human population of Kashmir valley to evaluate the status of the biochemical parameters of infected population. Materials and Methods: Blood samples were collected from 514 individuals, 298 (57.97%) males and 216 (42.02%) females, 187 (36.38%) were found sero-positive for human toxocariasis. Results: Alkaline phosphatase level was found highe...
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Introduction: Hydatid cyst disease is caused by the protoscolices of Echinococcus granulosus. Alkaline phosphatase (ALP) enzyme is required for metabolism, physiology, immunology, and nutrients absorption in parasite. The aim of this study was to compare the level of ALP activity (as a pathological biomarker) in hydatid cyst protoscolices (HCP) with that of sheep liver tissue and to determine t...
متن کاملPurification 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...
متن کاملQuantification and comparison of bone-specific alkaline phosphatase with two methods in normal and paget’s specimens
Background: Bone-specific alkaline phosphatase (BAP) is synthesized by the osteoblasts and is presumed to be involved in the calcification of bone matrix, though its precise role in the formation process is unknown. The aim of the present study was to measure the BAP activity in Paget's and normal specimens by two different techniques. Methods: Total ALP (TAP) as well as BAP activity-measuring ...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1998
ISSN: 0378-1097,1574-6968
DOI: 10.1111/j.1574-6968.1998.tb12940.x