scholarly journals HETEROGENEITY OF THE INHERITED GROUP-SPECIFIC COMPONENT OF HUMAN SERUM

1964 ◽  
Vol 120 (1) ◽  
pp. 83-91 ◽  
Author(s):  
Alexander G. Bearn ◽  
F. David Kitchin ◽  
Barbara H. Bowman
Keyword(s):  
Human Serum ◽  
Gel Electrophoresis ◽  
Polypeptide Chain ◽  
Buffer System ◽  
Starch Gel Electrophoresis ◽  
Specific Component ◽  
Agar Gel ◽  
Main Band ◽  
Starch Gel ◽  
Normal Human

Heterogeneity of the group-specific (Gc) components in normal human serum has been demonstrated by the use of a lithium borate buffer system in conventional vertical starch gel electrophoresis and by prolonged immunoelectrophoresis in agar gel. In both Gc 1-1 and Gc 2-2 phenotypes a protein component migrates ahead of the main band. Immunological evidence indicates that the faster migrating band contains Gc specificity. The possibility that the two electrophoretically distinct Gc components share a common polypeptide chain is discussed.

Ultrasonic Effects on lsoenzymes

1966 ◽  
Vol 12 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Clyde A Dubbs
Keyword(s):  
Human Serum ◽  
Ultrasonic Treatment ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Serum Cholinesterase ◽  
Starch Gel Electrophoresis ◽  
Selective Activation ◽  
Intracellular Enzymes ◽  
Starch Gel

Abstract Several significant effects of ultrasonic treatment on human serum cholinesterase and aminopeptidase isoenzymes and on other serum proteins have been found by starch gel electrophoresis. The selective activation of one cholinesterase isoenzyme is especially striking. These effects must be considered when ultrasonic treatment is used for the extraction of intracellular enzymes. When the effects are appreciated, ultrasonics should provide a valuable tool for isoenzyme research.

scholarly journals Hemoglobin Hope: A Beta Chain Variant

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 830-838 ◽  
Author(s):  
VIRGINIA MINNICH ◽  
ROBERT J. HILL ◽  
PHILIP D. KHURI ◽  
MARY E. ANDERSON
Keyword(s):  
Blood Cells ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Beta Chain ◽  
Agar Gel ◽  
Hemoglobin A ◽  
Abnormal Hemoglobin ◽  
Starch Gel ◽  
Agar Gel Electrophoresis ◽  
Chain Variant

Abstract A new hemoglobin, hemoglobin Hope, with a beta chain abnormality has been found in three generations of a St. Louis Negro family. The abnormal hemoglobin in the heterozygous state caused neither clinical stigmata nor abnormality in the red blood cells. Hemoglobin Hope was detected by agar gel electrophoresis at pH 6.2, but could not be differentiated from hemoglobin A by starch block electrophoresis at pH 8.6. Also, it could not be separated from hemoglobin A by paper, or starch gel electrophoresis employing a range of buffers from pH 6.2 to 8.6. Amino acid analysis showed that aspartic acid was substituted for glycine at position 136 of the beta chain. Hemoglobin Hope may be formulated as α2Aβ2136 gly-asp.

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 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 Separation of Insect Haemolymph Proteins

1964 ◽  
Vol 96 (1-2) ◽  
pp. 110-110
Author(s):  
B. G. Loughton ◽  
P. Rueffel ◽  
H. Stich ◽  
A. S. West
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Homologous Proteins ◽  
Agar Gel ◽  
Diffusion Technique ◽  
Starch Gel ◽  
Rapid Characterization ◽  
Gel Diffusion

It has been suggested that information on the phylogenetic relationships of genera and species could be obtained by comparing the amino acid sequence in the homologous proteins of different species. This procedure is extremely difficult and time-consuming.However, a relatively rapid characterization of proteins can be obtained by analysing their mobilities with starch-gel electrophoresis and examination of antigenic diversity by the agar gel diffusion technique of Ouchterlony.

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