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pro vyhledávání: '"Ewa Luchter-Wasylewska"'
Publikováno v:
Journal of Colloid and Interface Science. 273:632-637
The kinetics of 1-naphthyl phosphate and phenyl phosphate hydrolysis, catalyzed by human prostatic acid phosphatase (PAP) entrapped in AOT–isooctane–water reverse micelles, has been studied over surfactant hydration degree (w0) range 5 to 35. Con
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 35:1645-1657
Rhodanese (EC 2.8.1.1.) from bovine liver contains four reduced cysteine groups. The –SH group of cysteine 247, located in a rhodanese active centre, transfers sulfane sulfur in a form of hydrosulfide (–S–SH) from appropriate donors to nucleoph
Autor:
Ewa Luchter-Wasylewska
Publikováno v:
Analytical Biochemistry. 241:167-172
A continuous spectrophotometric assay for the determination of the initial rate of an acid phosphatase-catalyzed reaction in an acidic environment, using phenyl phosphate as a substrate, is presented. The method is based on the continuous determinati
Publikováno v:
Journal of protein chemistry. 22(3)
The apparent molecular mass of human prostatic acid phosphatase (PAP) was estimated over a wide range of enzyme concentrations using equilibrium centrifugation in the “Airfuge” tabletop ultra-centrifuge. We show that the average mass of all activ
Autor:
Ewa Luchter-Wasylewska
Publikováno v:
Biochimica et biophysica acta. 1548(2)
The steady-state kinetics of hydrolysis reaction catalysed by human prostatic acid phosphatase (PAP) by using 1-naphthyl phosphate, phenyl phosphate and phosphotyrosine as substrates has been studied at pH 5.5. The substrate binding curves were sigmo
Publikováno v:
IUBMB Life. 59:791-792
Is There An Answer? is intended to serve as a forum in which readers to IUBMB Life may pose questions of the type that intrigue biochemists but for which there may be no obvious answer or one may be available but not widely known or easily accessible
Autor:
Ewa Luchter-Wasylewska
Publikováno v:
Acta biochimica Polonica. 44(4)
The described continuous acid phosphatase assay is based on kinetics of the release of 1-naphthol in the course of the enzyme-catalyzed hydrolysis of 1-naphthyl phosphate, measured at 320 nm in aqueous solution and at 322 nm in sodium-bis(2-ethylhexy