Dimeric nature and amino acid compositions of homogeneous canine prostatic, human liver and rat liver acid phosphatase isoenzymes. Specificity and pH-dependence of the canine enzyme

Saini, Mohan S.; Etten, Robert L. Van

doi:10.1016/0005-2744(78)90138-9

Cited by 39 publications

(7 citation statements)

References 28 publications

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“…The assay was carried out at 30°C by adding 50 l of the enzyme solution to a reaction mixture containing 10 mM target substrate and 50 mM Tris maleate (pH 6.0), and phosphorus released during the 2 min incubation was measured according to a method described previously (18). In all assays one unit of enzyme activity was defined as 1 mol of P i released/min.…”

Section: Methodsmentioning

confidence: 99%

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: Methodsmentioning

confidence: 99%

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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“…Studies of the effect of pH on Km of prostatic acid phosphatase [18] show Km to be nearly independent of pH until the latter greatly exceeds 8.0. [7,8], an odd number of reactive thiols is unlikely unless the pro tein exhibits considerable negative co-operativity in respect of thiol reactivity. Negative co-operativity does not seem to have been reported for any acid phosphatases.…”

Section: Acid Phosphatasementioning

confidence: 99%

“…If the enzyme has an aß structure, an odd number of thiol groups is permissible and heterogene ity on electrophoresis provides support for the notion that PI has dissimilar subunits. The possibility must also be considered that the heterogeneity arises from limited proteo lysis occurring during the isolation of the enzyme, since other authors describe an a2 structure for PI [7,8].…”

Section: Acid Phosphatasementioning

confidence: 99%

“…Amino acid analysis of PI [7] figure 5 intersect the vertical axis at 1. It seems therefore that fast-reacting groups that may be modified without a loss of activ ity are absent.…”

Section: Acid Phosphatasementioning

confidence: 99%

“…Arginine residues may also be important in some forms of acid phosphatase [5], Of these various residues implicated in catalysis, a definite role has fluorescein mercuriacetate (FMA) in at tempts to determine the number of reactive thiols and to categorise them according to reactivity and importance for catalytic func tion. This enzyme of relative molecular mass 92,000 is reported to be a dimer of 51,000-dalton subunits [7,8], that had been inactivated (by approximately 50%) by PCMB treatment. A sample of PI that had been incu bated under identical conditions except for the ab sence of PCMB was used as a comparison.…”

Section: Introductionmentioning

confidence: 99%

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Reactive Thiol Groups in Rat Liver Acid Phosphatase

Navaratnam¹,

Banner²,

Butterworth³

1985

Enzyme

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Dimeric rat liver acid phosphatase PI of Mr 92,000 is inactivated by ρ-chloromercuribenzoate and fluorescein mercuriacetate (FMA). The enzyme is protected against the mercurials by the substrate analogue P(i). The reaction with FMA is accompanied by changes in absorbance at 495 nm and in fluorescence emission at 520 nm that are characteristic of reaction of this compound with thiol groups. Titration of PI with FMA monitored by spectrophotometry or by fluorimetry indicated that equivalence is reached at an FMA/P1 ratio of 3. Since FMA can act as a bifunctional reagent, it is likely that PI contains either 3 or 6 reactive thiol groups per molecule. Analysis of FMA inactivation/modification data by a statistical method suggests that of 6 reactive thiol groups, 2 are essential so that there are probably 3 thiol groups per subunit, one of which is located at the active site. If the total thiol number is 3, analysis suggests 1 essential thiol per subunit.

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Identification of Arginine Esterase as the Major Androgen‐dependent Protein Secreted by Dog Prostate and Preliminary Molecular Characterization in Seminal Plasma

Chapdelaine

Dubé

Frenette

et al. 1984

Journal of Andrology

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This work was undertaken to determine the identity of the major androgen-dependent 15,000 molecular weight protein previously observed on SDS polyacrylamide gel electrophoresis of both dog prostate cytosol and dog seminal plasma. The protein was identified as one of the two chains of arginine esterase on the basis of its ability to bind 3H-diisopropylphosphofluoridate (DFP), an active site titrant of serine proteases. Furthermore, since the other polypeptide chain was heterogeneous, at least five distinct peaks of arginine esterase activity could be separated by chromatofocusing under nonreducing conditions. The molecular weight of the seminal plasma protein was estimated at 29,500 by Sephadex G-100 gel filtration, and at 25,000 by SDS polyacrylamide gel electrophoresis in the absence of mercaptoethanol. In the presence of mercaptoethanol, two major peaks were observed with molecular weights of 15,000 and 14,000. These results show that arginine esterase of dog seminal plasma is a serine protease composed of two different chains linked by disulfide bridges. One of the chains contains the reactive serine group. The other one is probably glycosylated since it presents several isoelectric points.

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Dimeric nature and amino acid compositions of homogeneous canine prostatic, human liver and rat liver acid phosphatase isoenzymes. Specificity and pH-dependence of the canine enzyme

Cited by 39 publications

References 28 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

Reactive Thiol Groups in Rat Liver Acid Phosphatase

Identification of Arginine Esterase as the Major Androgen‐dependent Protein Secreted by Dog Prostate and Preliminary Molecular Characterization in Seminal Plasma

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