Purification and characterization of acid phosphatase from yellow lupin (Lupinus luteus) seeds

Olczak, Mariusz; Watorek, W; Morawiecka, Bronisława

doi:10.1016/s0167-4838(97)00055-1

Cited by 48 publications

(41 citation statements)

References 35 publications

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“…The plant ACPs are mostly dimeric glycoproteins, about 110 kDa per homodimer (14,23) or heterodimer. Similarly, heterogeneity in the molecular masses of the subunits of plant ACPs has also been reported for yellow lupin (24), sunflower seed (25), sycamore seeds (26), and tomato (27), reflecting partial proteolysis of a polypeptide chain or a change in the glycosylation pattern.…”

Section: Fig 3 Acp and Cpo Activities Of The Vanadate-substituted Ementioning

confidence: 65%

Characterization of a Novel Acid Phosphatase from Embryonic Axes of Kidney Bean Exhibiting Vanadate-dependent Chloroperoxidase Activity

Yoneyama

Shiozawa

Nakamura

et al. 2004

Journal of Biological Chemistry

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A novel colorless acid phosphatase (KeACP), which was distinct from the kidney bean purple acid phosphatase, was purified to apparent homogeneity and cloned from embryonic axes of kidney bean (Phaseolus vulgaris L. Ohfuku) during germination. When orthovanadate (VO 4 ؊3 ) is added to the apo form of the enzyme, KeACP uniquely exhibits the chloroperoxidase activity with loss of phosphatase activity. This is the first demonstration that KeACP is a vanadate-dependent chloroperoxidase in plants to be characterized and suggests that KeACP may play a role in modifying a wide variety of chlorinated compounds that are present in higher plants. The enzyme is a dimer that presents three forms made up of the combination of the dominant 56-kDa and the minor 45-kDa subunits, and both subunits contain carbohydrate. The full-length cDNA of the KeACP gene is 1641 nucleotides, and this sequence is predicted to encode a protein having 457 amino acid residues (52,865 Da), including a signal peptide. The complete nucleotide sequence of the genomic DNA (3228 bp) of KeACP consists of seven exons and six introns. Northern blot analysis demonstrated that the KeACP gene was expressed specifically in embryonic axes of the kidney bean, and its expression coincided with elongation of the embryonic axis during germination.

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Section: Fig 3 Acp and Cpo Activities Of The Vanadate-substituted Ementioning

confidence: 65%

Characterization of a Novel Acid Phosphatase from Embryonic Axes of Kidney Bean Exhibiting Vanadate-dependent Chloroperoxidase Activity

Yoneyama

Shiozawa

Nakamura

et al. 2004

Journal of Biological Chemistry

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“…However, the significance of activity against these metabolites would necessitate further investigation. It should be noted that β-glycerophosphate has been used as a non-physiological substrate (Olczak et al, 1997;Panara et al, 1994;Penheiter et al, 1997;Torriani, 1960) to test the activity of various phosphatases.…”

Section: Sno Substratesmentioning

confidence: 99%

Prediction of substrate specificity and preliminary kinetic characterization of the hypothetical protein PVX_123945 from Plasmodium vivax

Srinivasan

Nagappa

Shukla

et al. 2015

Experimental Parasitology

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“…APases have been suggested to interact non-specifically with other proteins, this being reflected in their chromatographic behavior (Olczak et al 1997). We have previously reported that most of the APase activity eluted as a major, single activity peak after Mono S column chromatography at pH 4.5 (Andriotis and Ross 2003).…”

Section: Multiple Apase Isozymes Exist In Hazel Seedsmentioning

confidence: 99%

“…phytases, phosphoglycolate phosphatase, 3-phosphoglycerate phosphatase (Duff et al 1994). Furthermore, constraints in determining the subcellular localisation of APases, their low abundance in plant tissues and their instability in dilute solutions make purification attempts and assignment of a clear physiological role difficult (Olczak et al 1997).…”

Section: Introductionmentioning

confidence: 99%

Isolation and partial characterisation of acid phosphatase isozymes from dormant oilseed of Corylus avellana L.

Andriotis

Ross

2004

Planta

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The acid phosphatase (orthophosphoric-monoester phosphohydrolase, EC 3.1.3.2) complement from dormant hazel (Corylus avellana L.) seeds was found to exhibit significant electrophoretic heterogeneity partially attributable to the presence of distinct molecular forms. In axiferous tissue, total acid phosphatase activity increased in a biphasic fashion during chilling, a treatment necessary to alleviate seed dormancy. Three acid phosphatase isozymes were isolated from cotyledons of dormant hazel seeds by successive ammonium sulphate precipitation, size-exclusion, Concanavalin A affinity, cation- and anion-exchange chromatographies resulting in 75-, 389- and 191-fold purification (APase1, APase2, APase3, respectively). The three glycosylated isoforms were isolated to catalytic homogeneity as determined by electrophoretic, kinetic and heat-inactivation studies. The native acid phosphatase complement of hazel seeds had an apparent Mr of 81.5 +/- 3.5 kDa as estimated by size-exclusion chromatography, while the determined pI values were 5.1 (APase1), 6.9 (APase2) and 7.3 (APase3). The optimum pH for p-nitrophenyl phosphate hydrolysis was pH 3 (APase1), pH 5.6 (APase2) and pH 6 (APase3). The hazel isozymes hydrolysed a variety of phosphorylated substrates in a non-specific manner, exhibiting low Km and the highest specificity constant (Vmax/ Km) for pyrophosphate. They were not primary phytases since they could not initiate phytic acid hydrolysis, while APase2 and APase3 had significant phospho-tyrosine phosphatase activity. Inorganic phosphate was a competitive inhibitor, while activity was significantly impaired in the presence of vanadate and fluoride.

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Purification and characterization of acid phosphatase from yellow lupin (Lupinus luteus) seeds

Cited by 48 publications

References 35 publications

Characterization of a Novel Acid Phosphatase from Embryonic Axes of Kidney Bean Exhibiting Vanadate-dependent Chloroperoxidase Activity

Characterization of a Novel Acid Phosphatase from Embryonic Axes of Kidney Bean Exhibiting Vanadate-dependent Chloroperoxidase Activity

Prediction of substrate specificity and preliminary kinetic characterization of the hypothetical protein PVX_123945 from Plasmodium vivax

Isolation and partial characterisation of acid phosphatase isozymes from dormant oilseed of Corylus avellana L.

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