OCCURRENCE OF PARALBUMINEMIA IN MULE

1963 ◽  
Vol 41 (9) ◽  
pp. 2025-2028 ◽  
Author(s):  
A. Amin ◽  
K. D. Shamloo
Keyword(s):  
Serum Albumin ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Agar Gel ◽  
Starch Grain ◽  
Starch Gel

One case of "double albuminemia" has been found among a total number of 70 mule sera tested. This condition was demonstrable by means of paper, agar gel, starch grain, and starch gel electrophoresis. Double albuminemia was shown to be present at pH's 8.6, 11.3, and 12.2. When tested immunochemically, however, these two albumins were alike, and were similar to normal mule serum albumin.

OCCURRENCE OF PARALBUMINEMIA IN MULE

1963 ◽  
Vol 41 (1) ◽  
pp. 2025-2028
Author(s):  
A. Amin ◽  
K. D. Shamloo
Keyword(s):  
Serum Albumin ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Agar Gel ◽  
Starch Grain ◽  
Starch Gel

One case of "double albuminemia" has been found among a total number of 70 mule sera tested. This condition was demonstrable by means of paper, agar gel, starch grain, and starch gel electrophoresis. Double albuminemia was shown to be present at pH's 8.6, 11.3, and 12.2. When tested immunochemically, however, these two albumins were alike, and were similar to normal mule serum albumin.

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.

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.

STUDIES ON THE LIVETINS OF EGG YOLK: III. HETEROGENEITY AND IMMUNOELECTROPHORETIC BEHAVIOR OF BETA-LIVETIN

1966 ◽  
Vol 44 (10) ◽  
pp. 1357-1364 ◽  
Author(s):  
Shun-Fong Hui ◽  
R. H. Common
Keyword(s):  
Serum Albumin ◽  
Gel Electrophoresis ◽  
Egg Yolk ◽  
The Other ◽  
Positive Staining ◽  
Staining Reaction ◽  
Starch Gel Electrophoresis ◽  
Hen’S Egg ◽  
Starch Gel ◽  
The One

Starch-gel electrophoresis of the total livetins of hen's egg yolk resolved 16 zones: seven major zones, six minor zones, and three faint, diffuse zones. One zone was identified with the major component of paper electrophoretic alpha-livetin and hence with serum albumin. Four of the major zones were identified with the major components of paper electrophoretic beta-livetin on the one hand, and with an electrophoretically heterogeneous livetin antigen (livetin antigen 3) on the other hand, thus establishing the electrophoretic heterogeneity and relative immunological homogeneity of the paper electrophoretic beta-livetin fraction. The other two major starch-gel electrophoretic zones were identified as transferrins by their positive staining reaction for iron and comparison of their mobilities with two corresponding serum starch-gel fractions.

A Simple Microelectrophoretic Method Using Starch-Agar Gel

1964 ◽  
Vol 10 (1) ◽  
pp. 62-68 ◽  
Author(s):  
Tatsuo Hase
Keyword(s):  
Quantitative Analysis ◽  
Ultraviolet Light ◽  
Gel Electrophoresis ◽  
Protein Analysis ◽  
Starch Gel Electrophoresis ◽  
Protein Patterns ◽  
Agar Gel ◽  
Starch Gel ◽  
Agar Gel Electrophoresis ◽  
Starch Agar

Abstract A simple microelectrophoretic method of protein analysis using the gel of starch agar mixture is described. The method is easily standardized and the results show consistency and reproducibility. Protein patterns obtained show higher resolution than those of paper or agar-gel electrophoresis and simulate that of starch-gel electrophoresis. Developed protein patterns are suitable to quantitative analysis by appropriate electrophotometric or ultraviolet-light scanning devices and can be preserved as permanent records.

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.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

scholarly journals THE INHERITANCE OF ENZYME VARIANTS FOR TYROSINE AMINOTRANSFERASE, NADP-DEPENDENT MALATE DEHYDROGENASE, NADP-DEPENDENT ISOCITRATE DEHYDROGENASE, AND TETRAZOLIUM OXIDASE IN TETRAHYMENA PYRIFORMIS, SYNGEN 1

Genetics ◽  
1973 ◽  
Vol 74 (4) ◽  
pp. 595-603
Author(s):  
D Borden ◽  
E T Miller ◽  
D L Nanney ◽  
G S Whitt
Keyword(s):  
Detailed Analysis ◽  
Malate Dehydrogenase ◽  
Isocitrate Dehydrogenase ◽  
Gel Electrophoresis ◽  
Tetrahymena Pyriformis ◽  
Tyrosine Aminotransferase ◽  
Breeding Program ◽  
Starch Gel Electrophoresis ◽  
Enzyme Locus ◽  
Starch Gel

ABSTRACT The isozymic patterns of tyrosine aminotransferase, NADP malate dehydrogenase, NADP isocitrate dehydrogenase, and tetrazolium oxidase were examined by starch-gel electrophoresis in Tetrahymena pyriformis, syngen 1. The genetics of the alleles controlling these enzymes was studied through a breeding program. Each enzyme locus was shown to assort vegetatively, as do other loci in this organism. A detailed analysis of the assortment process for the tyrosine aminotransferase locus indicated that the rate of stabilization of heterozygotes into pure types was essentially identical to previously-reported rates for other loci.

Sign in / Sign up

Export Citation Format

Share Document