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Scandinavian journal of clinical and laboratory investigation, 59(8), 593-606 (2000-02-26)
The importance of separation and identification of serum alkaline phosphatase (ALP; E.C. 3.1.3.1) fractions/isoenzymes has been frequently reported. Each serum ALP fraction/isoenzyme quantitation has both practical and theoretical importance. In the present work, serum was collected from Wistar rats and
Journal of enzyme inhibition and medicinal chemistry, 17(5), 345-350 (2003-04-10)
Uric acid inhibited 50% of the activity of bovine kidney low molecular mass phosphotyrosine protein phosphatase at concentrations of 1.0, 0.4, 1.3, and 0.2 mM, respectively for p-nitrophenyl phosphate (p-NPP), flavine mononucleotide, beta-naphthyl phosphate and tyrosine phosphate (Tyr-P) as substrates.
Biochemistry, 38(3), 914-922 (1999-01-20)
Most transmembrane, receptor-like protein-tyrosine phosphatases (RPTPs) contain two cytoplasmic catalytic protein-tyrosine phosphatase (PTP) domains, of which the membrane-proximal domain, D1, contains the majority of the activity, while the membrane-distal domain, D2, exhibits little or no activity. We have investigated the
Biochemistry and molecular biology international, 41(6), 1201-1208 (1997-05-01)
A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0.
Bio-protocol, 7(7), e2202-e2202 (2017-04-05)
Induction and secretion of acid phosphatase (APase) is a universal adaptive response of higher plants to low-phosphate stress ( Tran et al., 2010 ). The intracellular APases are likely involved in the remobilization and recycling of phosphate (Pi) from intracellular
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