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.

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 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

1-naphthyl phosphate: specifications for high-quality substrate for measuring prostatic acid phosphatase activity.

1982 ◽  
Vol 28 (1) ◽  
pp. 212-215 ◽  
Author(s):  
J L Bowers ◽  
G N Bowers
Keyword(s):  
Liquid Chromatography ◽  
Acid Phosphatase ◽  
Inorganic Phosphate ◽  
High Performance ◽  
Activity Concentration ◽  
Prostatic Acid Phosphatase ◽  
Phosphate Content ◽  
High Quality ◽  
Kinetic Measurements ◽  
Simultaneous Comparisons

Abstract Ten lots of sodium 1-naphthyl phosphate were compared by spectrophotometry, high-performance liquid chromatography, and kinetic measurements of the activity of human prostatic acid phosphatase (EC 3.1.3.2) in serum. Two lots were readily identified as the 2-naphthyl phosphate salt by spectrophotometry and liquid chromatography. Four of the remaining eight lots of sodium 1-naphthyl phosphate met the following specifications: (a) sodium 1-naphthyl phosphate content greater than 80% by A286nm measurements (epsilon286nm1-NP = 5630 L.mol-1.cm-1) and by enzymic conversion to 1-naphthol (epsilon332nm1-N = 7560 L.mol-1.cm-1), (b) free 1-naphthol less than 3 mmol/mol, (c) inorganic phosphate less than 10 mmol/mol, and (d) the catalytic activity concentration greater than 98% maximum by absorbance assay and greater than 90% maximum by spectrofluorometric assay during simultaneous comparisons of several substrates. The need for detailed specifications and the testing of each batch of sodium 1-naphthyl phosphate is readily demonstrated by this study.

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.

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