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Phytochemistry. 1998 Nov 20;49(6):1517-1523.

Purification and properties of pi-repressible acid phosphatases from Aspergillus nidulans.

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1
Departamento de Química, FFCLRP-USP, 14040-901,., Ribeirão Preto, Brazil

Abstract

Two forms of the pacA-encoded acid phosphatase (designated acid phosphatases I and II) secreted by the mold Aspergillus nidulans grown in low-Pi medium at 37 degrees, pH5.0, were purified to apparent homogeneity by PAGE. The M(r) of the purified enzyme forms were ca 115000 (60000) and 113000 (62000) respectively for forms I and II secreted by strain biA1 and ca 118000 (60000) and 121000 (61000) respectively for forms I and II secreted by strain biA1 pacA1, as determined by exclusion chromatography (number between brackets are the M(r) as determined by SDS-PAGE). All of these purified enzyme forms showed an apparent optimum pH ranging from 6.0 to 6.5 and no deviation from Michaelis kinetics for the hydrolysis of both p-nitrophenylphosphate and alpha-naphthylphosphate. Heat inactivation at 60 degrees and at pH6.0 showed half-lives of 14min (k=0.033min(-1)) and 10min (k=0.069min(-1)), respectively, for the purified acid phosphatases I and II secreted by biA1 strain and half-lives of 0.8min (k=0.92min(-1)) and 0.6min (k=0.95min(-1)), respectively, for the purified forms I and II secreted by the biA1 pacA1 strain. The neutral sugar content of purified acid phosphatases I and II secreted by strain biA1 was 48% and 37% (w/w), respectively, whereas the content of forms I and II secreted by strain biA1 pacA1 was 18% and 11%, respectively.

PMID:
11711060
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