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Partial purification and some biochemical properties of acid phosphatase in germinating chickpea ( Cicer arietinum ) seeds
Author(s) -
Angosto T.,
González F.,
Matilla A.
Publication year - 1988
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1988.tb02042.x
Subject(s) - dithiothreitol , chemistry , hydrolysis , polyacrylamide gel electrophoresis , arsenate , biochemistry , phosphate , phosphatase , chromatography , enzyme , acid phosphatase , gel electrophoresis , ammonium , organic chemistry , arsenic
An acid phosphatase (EC 3.1.3.2.) from the embryonic axes of chickpea seeds ( Cicer arietinum L. cv. Castellana) was purified by ammonium sulphate precipitation, chromatography on Sephacryl S‐200 and polyacrylamide gel electrophoresis. The preparation has an apparent molecular weight of 39 kDa, pH optimum for p ‐nitrophenylphosphate hydrolysis of 5.25, and K m of 0.57 m M . The enzyme hydrolyzed all the mono‐ and di‐phosphorylated sugars tested, but had no effect on ATP, ADP, AMP and phosphoenolpyruvate. Phosphate was a competitive inhibitor. Mg 2+ . Ca 2+ , Hg 2+ , Fe 3+ , arsenate, K + and Zn 2+ were inhibitory. Mn 2+ , dithiothreitol and EDTA had no effect, and polyamines were activators.