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.
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
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
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.
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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