1988
DOI: 10.1111/j.1399-3054.1988.tb02042.x
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Partial purification and some biochemical properties of acid phosphatase in germinating chickpea (Cicer arietinum) seeds

Abstract: 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 Km of 0.57 mM. The enzyme hydrolyzed all the mono‐ and di‐phosphorylated sugars tested, but had no effect on ATP, ADP, AMP and phosphoenolpyruvate. Phosphate … Show more

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Cited by 12 publications
(7 citation statements)
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“…5). The optimum pH of the Apases purified from plant tissues differed depending on the plant species and tissues, with value ranging from pH 4 to pH 6 (Hasegawa et al 1976;Mclachlan 1980;Dracup et al 1984;Angosto et al 1988;Tanaka et al 1990). The optimum pH of Apase-T also appeared to be in this range and was very similar to the optimum pH of Apase purified from cultured tobacco cells (Ninomiya et al 1977).…”
Section: 5mentioning
confidence: 99%
See 1 more Smart Citation
“…5). The optimum pH of the Apases purified from plant tissues differed depending on the plant species and tissues, with value ranging from pH 4 to pH 6 (Hasegawa et al 1976;Mclachlan 1980;Dracup et al 1984;Angosto et al 1988;Tanaka et al 1990). The optimum pH of Apase-T also appeared to be in this range and was very similar to the optimum pH of Apase purified from cultured tobacco cells (Ninomiya et al 1977).…”
Section: 5mentioning
confidence: 99%
“…Apase-L showed a higher relative activity for UTP, CTP, and lysolecithin than Apase-T, whereas, Apase-T showed a higher relative activity for D-myo-inositol-l,4,5-tris-phosphate than Apase-L. Glycerolphosphate, glucose and fructose phosphate, NADP, and inositol-l,3,4,5-tetraphosphate were not hydrolyzed by both Apases. It has been documented that the Apases purified from plant tissues display a broad substrate specificity, which enabled to hydrolyze nucleotides, phospholipids and sugar phosphates, but not phytin (Shaw 1966;Ching et al 1987;Dua and Amma 1987;Angosto et al 1988;Kaneko et al 1990). The secretory Apase also showed a similar broad substrate specificity.…”
Section: 5mentioning
confidence: 99%
“…The optimum pH was 4.3, which is ecologically significant because it indicates that the enzyme performs well in low pH soils where the availability of phosphate is mostly limited. As the optimum pH of acid phosphatase of the plants reported ranged from 4.5 to 6.0 (Basha 1984;Ching et al 1987;Angosto et al 1988;Kaneko et al 1990;Ullah and Gibson 1988;Tanaka et al 1990;Yoshimoto et al 1992), secreted acid phosphatase from lupin roots appeared to be adapted to much lower pH conditions.…”
Section: H a R A C T E R I S T I C S Of S E C R E T E D A C I D P Hmentioning
confidence: 99%
“…2A, inset). This suggests that the axis exercises some sort of control over ACC-synthase production, just as it does in other metabolic activities (2,21). Supraoptimal temperatures appear to stimulate ACC-synthase activity (Fig.…”
Section: Discussionmentioning
confidence: 99%