scholarly journals Immunochemical differences in acid phosphatase isozymes from wheat germ.

1986 ◽  
Vol 50 (2) ◽  
pp. 437-440 ◽  
Author(s):  
Takashi AKIYAMA ◽  
Shigeru YAMAMOTO
Keyword(s):  
Acid Phosphatase ◽  
Wheat Germ

LA PHOSPHATASE ACIDE DU GERME DE BLÉ: ANALYSE CHROMATOGRAPHIQUE

1965 ◽  
Vol 43 (12) ◽  
pp. 1899-1905 ◽  
Author(s):  
Jacques Brouillard ◽  
Ludovic Ouellet
Keyword(s):  
Acid Phosphatase ◽  
Chromatographic Analysis ◽  
Wheat Germ ◽  
Molecular Forms ◽  
Phosphatase Acide ◽  
Visible Spectra

Chromatographic analysis of acid phosphatase of wheat germ shows that this enzyme exists as four different, active, and easily separable molecular forms. The four fractions also hydrolyze esterase substrates. All four isozymes are yellow, and the visible spectra of three of them are given. Following a previous observation, we confirmed the presence of iron in the enzyme, presumably as Fe+++.

scholarly journals Wheat Germ Acid Phosphatase Activity in High Percentages of Organic Solvents

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Veronica R. Moorman ◽  
Evan D. Kindl ◽  
Fiona N. Summers
Keyword(s):  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Organic Solvents ◽  
Acid Phosphatase Activity ◽  
Wheat Germ

scholarly journals Hydrolytic and alcoholytic dephosphorylation of nucleotides by acid phosphatase in the presence of ethanol

1971 ◽  
Vol 124 (1) ◽  
pp. 189-192 ◽  
Author(s):  
M. Tomaszewski ◽  
J. Buchowicz
Keyword(s):  
Acid Phosphatase ◽  
Inorganic Phosphate ◽  
Wheat Germ ◽  
Assay Mixture ◽  
Enzyme Substrates

The effect of ethanol on the activity of acid phosphatase from wheat germ was studied, by using ribonucleoside monophosphates as the enzyme substrates. The nucleotides were effectively degraded to the corresponding nucleosides in the presence of ethanol at all concentrations tested, including a 96% (v/v) solution. However, the nucleotide dephosphorylation was accompanied by the liberation of orthophosphate only when the concentration of ethanol in the assay mixture did not exceed 15%. No inorganic phosphate was liberated when ethanol was present at higher concentrations. Instead, monoethyl phosphate was formed in quantities expected for orthophosphate. The results are explained in terms of phosphatase-catalysed alcoholysis.

A rennin-sensitive bond in αs1Β-casein

1974 ◽  
Vol 41 (1) ◽  
pp. 147-153 ◽  
Author(s):  
R. D. Hill ◽  
E. Lahav ◽  
D. Givol
Keyword(s):  
Acid Phosphatase ◽  
Wheat Germ ◽  
Kinetic Constants ◽  
Similar Action ◽  
Basic Peptide

SummaryRennin acts on a specially sensitive bond in αs1B-casein to produce a basic peptide containing residues 1–23 of the original protein. At pH 6·4 and 30°C, the action is specific and rapid, the kinetic constants beingKm4·5×10−4M,Kcat3·8 s−1, andkcat/Km0·85×104s−1M−1. Pepsin, and a protease impurity in the acid phosphatase from wheat germ, have a similar action.

The enzymic deacylation of esterified mono- and di-saccharides. I. The isolation and purification of an esterase from wheat germ lipase

1969 ◽  
Vol 47 (2) ◽  
pp. 135-142 ◽  
Author(s):  
A. L. Fink ◽  
G. W. Hay
Keyword(s):  
Acid Phosphatase ◽  
Wheat Germ ◽  
Polyacrylamide Gel Electrophoresis ◽  
Disc Electrophoresis ◽  
Isolation And Purification ◽  
Electrophoretic Behavior ◽  
Commercial Enzymes ◽  
Cursory Examination ◽  
Different Sources ◽  
Molecular Sieving

Whereas wheat germ lipase was known to contain acid phosphatase (EC 3.1.3.2), esterase (EC 3.1.1.1), and lipase (EC 3.1.1.3) activity, a cursory examination of some commercial enzymes has demonstrated also the presence of phosphodiesterase (EC 3.1.4.1), α- and β-glucosidase (EC 3.2.1.20 and EC 3.2.1.21), α- and β-galactosidase (EC 3.2.1.22 and EC 3.2.1.23), α-mannosidase (EC 3.2.1.24), and β-xylosidase (EC 3.2.1.37) activities. Disc electrophoresis revealed a minimum of 12 electrophoretically distinct protein fractions. Different sources and different batches of enzyme had similar disc electrophoretic behavior and activities. Fractionation of the crude preparation on carboxymethylcellulose or Sephadex, and electrophoresis on Sephadex, failed to separate α-glucosidase and esterase activities. The inhibition of α- and β-glucosidase could be effected by D-glucono-1,5-lactone, but not by metal salts or Tris.Preparative polyacrylamide-gel electrophoresis of wheat germ lipase gave a large number of active zones including several esterases, acid phosphatase, and α- and β-glucosidase fractions. Evidence was established for the nonidentity of two neighboring esterase zones. One was found to be free of α- and β-glucosidase activity. Sulfhydryl reagents inhibited the esterases, whereas acetone activated some and inactivated others. The esterases were most stable at neutral pH and were extensively inactivated on lyophilization, dialysis, and desalting with molecular-sieving reagents. Some properties of the purified esterase were examined.

scholarly journals Simplified preparation of a phosphatase inhibitor and further studies of its action

1978 ◽  
Vol 171 (2) ◽  
pp. 485-488 ◽  
Author(s):  
S P Coburn ◽  
W E Schaltenbrand
Keyword(s):  
Alkaline Phosphatase ◽  
Acid Phosphatase ◽  
Wheat Germ ◽  
Kinase Activity ◽  
Phosphatase Inhibitor ◽  
Enzyme Systems

1-Pyrrolidinecarbothioic acid (2-pyridylmethylene) hydrazide chelates Zn2+ but not Mg2+. This compound is about twice as effective as EDTA for inhibiting alkaline phosphatase from calf mucosa, and approx. 1000-fold more effective than EDTA for inhibiting acid phosphatase from wheat germ. The compound did not inhibit pyridoxine kinase activity in human leucocytes at the highest concentration tested (33 micron). Therefore it may be a useful tool for either examining or eliminating the effects of phosphatases in complex enzyme systems.

scholarly journals Identification of individual components of a commercial wheat germ acid phosphatase preparation

PLoS ONE ◽  
2021 ◽  
Vol 16 (3) ◽  
pp. e0248717
Author(s):  
Veronica R. Moorman ◽  
Alexandra M. Brayton
Keyword(s):  
Acid Phosphatase ◽  
Wheat Germ ◽  
Purification Step ◽  
Active Components ◽  
Commercial Preparation ◽  
Purple Acid Phosphatases ◽  
Protein Components ◽  
Laboratory Tool ◽  
Shock Proteins ◽  
Post Purchase

Wheat germ acid phosphatase (WGAP) is a commercial preparation of partially purified protein commonly used in laboratory settings for non-specific enzymatic dephosphorylation. It is known that these preparations contain multiple phosphatase isozymes and are still relatively crude. This study therefore aimed to identify the protein components of a commercial preparation of wheat germ acid phosphatase using mass spectroscopy and comparative genomics. After one post-purchase purification step, the most prevalent fifteen proteins in the mixture included heat shock proteins, beta-amylases, glucoseribitol dehydrogenases, enolases, and an aminopeptidase. While not among the most abundant components, eight unique dephosphorylation enzymes were also present including three purple acid phosphatases. Furthermore, it is shown that some of these correspond to previously isolated isozymes; one of which has been also previously shown by transcriptome data to be overexpressed in wheat seeds. In summary, this study identified the major components of WGAP including phosphatases and hypothesizes the most active components towards a better understanding of this commonly used laboratory tool.

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