Quantitative Determination of Creatine Kinase Activity after Separation of Isoenzymes by Starch-Gel Electrophoresis

1973 ◽  
Vol 1 (3) ◽  
pp. 746-747
Author(s):  
R. L. WATTS ◽  
JANE EVE
Keyword(s):  
Creatine Kinase ◽  
Quantitative Determination ◽  
Gel Electrophoresis ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Starch Gel Electrophoresis ◽  
Starch Gel

Bioluminescence flow sensor for determination of creatine kinase activity in blood

1989 ◽  
Vol 227 ◽  
pp. 29-36 ◽  
Author(s):  
S. Girotti ◽  
M.L. Cascione ◽  
S. Ghini ◽  
G. Carrea ◽  
R. Bovara ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Flow Sensor

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 FLUORIMETRIC DETERMINATION OF CREATINE KINASE ACTIVITY IN ISOLATED SINGLE NEURONS

1973 ◽  
Vol 21 (6) ◽  
pp. 568-571 ◽  
Author(s):  
IGOR B. KRASNOV
Keyword(s):  
Creatine Kinase ◽  
Enzyme Activity ◽  
Coefficient Of Variation ◽  
Kinase Activity ◽  
Tissue Sample ◽  
Vestibular Nucleus ◽  
Creatine Kinase Activity ◽  
Single Neurons ◽  
Fluorimetric Determination

A quantitative fluorimetric method for determination of creatine kinase activity in isolated single nerve cells (2-10 ng dry weight) has been developed. Enzyme activity was measured in the direction of adenosine triphosphate and creatine formation. The creatine generated was measured by the fluorescent compound formed with ninhydrin in alkali. The coefficient of variation for the assay of enzyme activity in brain homogenate (47 ng wet tissue/sample) was 3.17%. The coefficient of variation for single neurons of the lateral vestibular nucleus (nucleus Deitersi) in rabbit was about 15%. The creatine kinase activity in these cell bodies was 342.0 ± 14.2 moles/kg dry tissue/hr, at 38°C.

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.

Evaluation of a New Procedure for Measuring Serum Creatine Kinase Activity

1970 ◽  
Vol 16 (5) ◽  
pp. 370-374 ◽  
Author(s):  
J Henry Wilkinson ◽  
B Steciw
Keyword(s):  
Creatine Kinase ◽  
Spectrophotometric Method ◽  
Kinase Activity ◽  
Creatine Phosphate ◽  
Sample Volume ◽  
Creatine Kinase Activity ◽  
Serum Creatine Kinase ◽  
Normal Range ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract A new spectrophotometric microtechnique for the determination of serum creatine kinase activity, in which all reagents are provided in a single com-pressed tablet, has been evaluated. The procedure depends upon coupling the creatine phosphate-ADP reaction with the hexokinase and glucose-6-phosphate dehydrogenase reactions. The new technique is quick, relatively simple, and gives results which compare favorably with the conventional spectrophotometric method in precision and sensitivity. It requires a sample volume of 10 Al, and values ranging from 10 to1600 U/liter can be determined without dilution. Gross hemolysis leads to erroneously high values, but the error is negligible with slightly hemolyzed specimens. A provisional normal range has been established

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