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.

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

Galanin in the normal human pituitary and brain and in pituitary adenomas

1991 ◽  
Vol 130 (3) ◽  
pp. 463-467 ◽  
Author(s):  
W. M. Bennet ◽  
S. F. Hill ◽  
M. A. Ghatei ◽  
S. R. Bloom
Keyword(s):  
Chromatographic Analysis ◽  
Gel Permeation Chromatography ◽  
Molecular Forms ◽  
Pituitary Tumours ◽  
Healthy Human ◽  
Human Pituitary ◽  
Gel Permeation ◽  
Normal Human ◽  
Wet Weight ◽  
Mean Concentration

ABSTRACT Galanin-like immunoreactivity (IR) was measured by radioimmunoassay in extracts of non-tumorous and tumorous human pituitaries and in multiple sites in the human brain. Galanin-IR was present in considerable quantities in the non-tumorous pituitaries (21·4±1·2 pmol/g wet weight; mean ± s.e.m., n = 30). In 25 pituitary tumours, galanin-IR was detectable in extracts of only nine, with a mean concentration of 11·5±4·4 pmol/g. Galanin-IR was undetectable in the remaining 16. Of ten brain sites, galanin-IR was detected only in the hypothalamus, where the concentration was 9·1±1·8 pmol/g (n = 5). On fast protein liquid chromatography of the non-tumorous pituitary extracts, galanin-IR mostly eluted in a peak with a retention time similar to that of synthetic porcine galanin. On gel permeation chromatography, galanin-IR eluted as a peak with an elution coefficient (Kav) of 0·72, also similar to that of porcine galanin, with additional preceding (Kav 0·62) and following (Kav 0·77) peaks of galanin-IR. These results show that healthy human pituitary and hypothalamus contain substantial amounts of galanin, whereas it is present in variable amounts or not at all in pituitary tumours. Chromatographic analysis suggests that pituitary galanin is present in three molecular forms, with the majority corresponding to synthetic porcine galanin. Journal of Endocrinology (1991) 130, 463–467

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.

scholarly journals Heterogeneity of the acid phosphatase and ribonuclease from protocorms of the orchids Cymbidium Sw. and changes occurring after treatment with streptomycin

2015 ◽  
Vol 42 (1) ◽  
pp. 133-141 ◽  
Author(s):  
B. Morawiecka ◽  
A. Kubicz ◽  
K. Kukułczanka ◽  
A. Koch ◽  
E. Markefka
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Culture Medium ◽  
Disc Electrophoresis ◽  
Molecular Forms ◽  
Stages Of Development ◽  
Early Stages ◽  
Electrophoretic Patterns ◽  
Culture Growth

The molecular forms of the acid phosphatase and RNase in protocorms of <i>Cymbidium</i> Sw. were studied by disc electrophoresis. The effect of streptomycin added to the culture medium on both enzymes was investigated. Significant changes in enzyme activity and electrophoretic patterns occured after addition of streptomycin at the beginning of culture growth. This indicates that the enzymes are affected by streptomycin in early stages of development of the protocorms.

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.

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