A QUANTITATIVE METHOD FOR THE DETERMINATION OF CHOLINESTERASE ACTIVITY AFTER STARCH-GEL ELECTROPHORESIS

1966 ◽  
Vol 44 (6) ◽  
pp. 953-955 ◽  
Author(s):  
H. S. Funnell ◽  
W. T. Oliver
Keyword(s):  
Gel Electrophoresis ◽  
Quantitative Method ◽  
Cholinesterase Activity ◽  
Competitive Inhibition ◽  
Starch Gel Electrophoresis ◽  
Final Solution ◽  
Natural Activity ◽  
Starch Gel ◽  
Hydrolysis Of

The method described in this paper is based upon hydrolysis of the starch gel by sodium hydroxide, which releases the dye. The dye is then taken up in an immiscible solvent, and the color determined spectrophotometrically. The method gave good reproducibility in studies both of natural activity and competitive inhibition without requiring any changes in the usual methods. The amount of dye in the final solution was related to the activity towards the dye-producing substrate of the enzyme present in the gel section.

Improved Method for the Determination of Hemoglobin A2 by Starch-Gel Electrophoresis

1960 ◽  
Vol 6 (3) ◽  
pp. 254-262 ◽  
Author(s):  
C A J. Goldberg ◽  
A C Ross
Keyword(s):  
Sickle Cell ◽  
Gel Electrophoresis ◽  
Sickle Cell Trait ◽  
Starch Gel Electrophoresis ◽  
Improved Method ◽  
Starch Gel ◽  
Thalassemia Trait ◽  
Healthy Persons ◽  
Hemoglobin A2

Abstract It has been shown that variations in the preparation of the starch gel and in photographic interpretation can significantly affect the accuracy of the measurement of hemoglobin A2. An improved method for the determination of hemoglobin A2 by starch-gel electrophoresis has been presented which affords greater accuracy than was previously achieved. Hemoglobin A2 concentrations for healthy persons and patients with sickle cell trait, various nonthalassemic anemias, and thalassemia trait have been presented.

A New Method for Starch Gel Electrophoresis of Human Hemoglobins, with Special Reference to the Determination of Hemoglobin A2

1958 ◽  
Vol 4 (6) ◽  
pp. 484-495 ◽  
Author(s):  
C A J Goldberg
Keyword(s):  
Special Reference ◽  
Gel Electrophoresis ◽  
New Method ◽  
Resolving Power ◽  
Buffer System ◽  
Starch Gel Electrophoresis ◽  
Healthy Individuals ◽  
Starch Gel ◽  
Hemoglobin A2

Abstract A method for starch gel electrophoresis of hemoglobins is presented in which a modified Lintner starch is used for the preparation of the gel. A discontinuous buffer system of tris-EDTA-borate/barbital is used as the electrolyte medium because of its superior resolving power. Hemoglobin A2 values, obtained with this method, of healthy individuals, patients with thalassemia, and those with various anemias of nonthalassemic origin are presented.

scholarly journals Organic pyrophosphates as substrates for human alkaline phosphatases

1967 ◽  
Vol 105 (3) ◽  
pp. 1307-1312 ◽  
Author(s):  
R. Helen Eaton ◽  
D W Moss
Keyword(s):  
Gel Electrophoresis ◽  
Human Liver ◽  
Inorganic Phosphate ◽  
Starch Gel Electrophoresis ◽  
Alkaline Phosphatases ◽  
Starch Gel ◽  
Pyrophosphatase Activity ◽  
Small Intestinal ◽  
Hydrolysis Of ◽  
Single Enzyme

1. Purified human liver and small-intestinal alkaline orthophosphatases release inorganic phosphate at appreciable rates from a variety of organic pyrophosphate substrates. 2. The pyrophosphatase action is inhibited by Mg2+ ions at concentrations that activate the hydrolysis of orthophosphate substrates by these enzymes. 3. The results of mixed-substrate experiments, denaturation studies with heat or urea and starch-gel electrophoresis suggest that both orthophosphatase and pyrophosphatase activities are, in each preparation, properties of a single enzyme. 4. Intestinal phosphatase shows greater pyrophosphatase activity relative to orthophosphatase than the liver enzyme.

scholarly journals The determination of lactate dehydrogenase isoenzymes in normal human muscle and other tissues

1967 ◽  
Vol 105 (2) ◽  
pp. 599-604 ◽  
Author(s):  
A. E. H. Emery
Keyword(s):  
Lactate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Human Muscle ◽  
Starch Gel Electrophoresis ◽  
Fibrous Connective Tissue ◽  
Starch Gel ◽  
Normal Human ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Good Agreement

1. A technique has been developed, based on preferential inhibition by urea, for determining the amounts and proportions of the M and H sub-units of lactate dehydrogenase (referred to as LDH-M and LDH-H respectively) in human tissues, including muscle. 2. There was good agreement between the results obtained with urea inhibition and those obtained with starch-gel electrophoresis. 3. With increasing age there was a significant decrease in the total amount of lactate dehydrogenase and the amount of LDH-M in skeletal muscle. This could not be accounted for by the replacement of functioning muscle tissue by fibrous connective tissue. 4. The proportion of LDH-M was less in certain muscles (e.g. soleus and extra-ocular) than in other muscles (e.g. gastrocnemius and rectus abdominis). 5. The proportions of LDH-M and LDH-H did not differ significantly in different superficial limb muscles and were not significantly affected by either age or sex. 6. Specimens of muscle from 86 different individuals (all Europeans) have been subjected to electrophoresis, but no variants of lactate dehydrogenase isoenzymes have been found.

The labelling of certain milk proteins with iodine131

1965 ◽  
Vol 32 (2) ◽  
pp. 181-186 ◽  
Author(s):  
H. A. Veringa ◽  
M. F. Kerkhof Mogot
Keyword(s):  
Gel Electrophoresis ◽  
Milk Proteins ◽  
Starch Gel Electrophoresis ◽  
Molecular Weights ◽  
Fat Globules ◽  
Starch Gel ◽  
Clustering Effect ◽  
Β Lactoglobulin ◽  
Electrophoresis Pattern

SummaryWhole casein, β-casein, β-lactoglobulin and euglobulin were labelled with 131I. The conditions under which iodination was carried out were chosen so as to avoid any modification of the original characteristics of the proteins. This was checked by starch-gel electrophoresis and determination of sedimentation constants, apparent molecular weights and, for euglobulin, the clustering effect on fat globules.As was shown by autoradiograms of the starch-gel plates, the radioactivity was incorporated in all zones of the electrophoresis pattern.

scholarly journals ENZYMES IN HOG KIDNEY HYDROLYZING AMINO ACID NAPHTHYLAMIDES

1966 ◽  
Vol 14 (4) ◽  
pp. 314-325 ◽  
Author(s):  
T. VANHA-PERTTULA ◽  
V. K. HOPSU ◽  
G. G. GLENNER
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Gel Electrophoresis ◽  
Metal Ion ◽  
Total Activity ◽  
Starch Gel Electrophoresis ◽  
Enzyme Preparations ◽  
Starch Gel ◽  
Hydrolysis Of ◽  
Hog Kidney

Hydrolysis of β-naphthylamides of a number of amino acids and dipeptides and of a number of di- and tripeptides by hog kidney homogenate and by fractions obtained by various fractionation procedures has been studied. The substrates were found to be split by a soluble, apparently sulfhydryl-dependent enzyme, and by a particle-bound, metal-activated enzyme. The former constituted only a small part of the total activity. The latter was subfractionated by starch gel electrophoresis into two fractions with identical characteristics. The soluble and particle-bound enzymes differed also in their substrate specificity. The latter enzyme was solubilized, partially purified, characterized by some modifier compounds and compared with enzyme preparations obtained by various fractionation procedures presented by other investigators. Thus enzyme showed ion-determined substrate specificity, i.e., hydrolysis of some of the amino acid naphthylamides was found to be activated by Co++ while the hydrolysis of others was inhibited by the same metal ion.

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