Apr 1, 1976

Study of acid phosphatase II from Pichia guilliermondii yeasts

Ukrainskiĭ biokhimicheskiĭ zhurnal
L P StrugovschikovaG M Shavlovskiĭ


Acid phosphatase II (AP II) was isolated from the cell-free extract of Pichia guilliermondii Wickerham ATCC 9058 and partially purified. The enzyme is a non-specific phosphomonoesterase. It hydrolyzes p-nitrohenyl-phophate (NPP), beta-glycerophosphate, glucose-6-phosphate, guanosine-5'-monophosphate, adenosine-5'-monophosphate, cytidine-5'-monophosphate, uridine-5'-monophosphate, alpha-naphtylphosphate, FMN. The order of the substrates corresponds to the degree of their hydrolysis decrease. The Michaelis constant of the enzyme was 1.4-10-3 M for NPP as a substrate, pH optimum was 5.5 and temperature optimum-40C. AP II was strongly inhibited by MoO4-2, F-, inorganic phosphate, Cu2+ and Be2+. The activity of the enzyme in the yeast cells does not change noticeably during growth on media with low and high iron content.

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Mentioned in this Paper

Acid Phosphatase
Chromatography, DEAE-Cellulose
Molecular Sieve Chromatography
Cell-Free System
Hydrogen-Ion Concentration
Enzyme Activation

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