scholarly journals Inheritable Differences in the Electrophoretic Pattern of Hemoglobin Revealed in a Local Random-Bred Colony of Albino Rats

Blood ◽  
1970 ◽  
Vol 35 (4) ◽  
pp. 447-450 ◽  
Author(s):  
JOVO V. MARTINOVIC ◽  
DOBRIVOJE V. MARINKOVIC ◽  
DUSAN T. KANAZIR ◽  
PETER N. MARTINOVITCH
Keyword(s):  
Gel Electrophoresis ◽  
Electrophoretic Pattern ◽  
Albino Rats ◽  
Buffer System ◽  
Starch Gel Electrophoresis ◽  
Parental Type ◽  
Starch Gel ◽  
F2 Generation

Abstract In a local colony of random-bred Albino rats, three different patterns of hemoglobin, arbitrarily denoted as patterns I, II and III, were detected by means of starch-gel electrophoresis in a discontinuous buffer system. Mating experiments showed that rats bearing pattern I and pattern III hemoglobin bred true. Crosses of pattern I with pattern III animals yielded only pattern II animals, and when the latter were mated inter se, the resultant F2 generation showed approximately a ratio of 1:2:1 for patterns I, II and III, respectively. When F1 animals from pattern I with pattern III crosses were mated back to animals of either parental type, the resultant ratio was found to be one pattern II: one pattern I or pattern III.

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.

Study of Mouse Hemoglobin by Starch-Gel Electrophoresis

1964 ◽  
Vol 13 (2) ◽  
pp. 185-189 ◽  
Author(s):  
T. N. Mehrotra ◽  
Giuseppe Cardinali
Keyword(s):  
Gel Electrophoresis ◽  
Adult Animal ◽  
Electrophoretic Pattern ◽  
Inbred Strains ◽  
Single Band ◽  
Starch Gel Electrophoresis ◽  
Inbred Strains Of Mice ◽  
Starch Gel ◽  
Band Type

SummaryThe hemoglobin pattern of 18 inbred strains of mice was studied by starch-gel electrophoresis. In 7 strains (C57BL/10, C57BL/6, C57BR/cd, C57L, C58, SWR, and SEC/1Re) the electrophoretic pattern was found to be of single-band type: in the remaining 11 strains (AKR, DBA/1, DBA/2, CBA, C3H/He, C3HeB/Fe, Fl/1Re, RF, 129, A, and A/He), 6 components were constantly observed when the electrophoretic run was carried out for 20 hours. Hemoglobin from late C57BL/6 fetuses showed an electrophoretic pattern identical to that of the adult animal. Hemoglobin from AKR and DBA/2 late fetuses and newborns showed an electrophoretic pattern similar to that of the adult animal, but the slowest band was more intensely stained as compared with the corresponding band of the adult animal.

scholarly journals LINKAGE ANALYSIS OF THE MULTILOCUS GLUCOSEPHOSPHATE ISOMERASE ISOZYME SYSTEM IN SUNFISH (CENTRARCHIDAE, TELEOSTII)

Genetics ◽  
1976 ◽  
Vol 82 (1) ◽  
pp. 35-42
Author(s):  
Gregory S Whitt ◽  
William F Childers ◽  
James B Shaklee ◽  
Janet Matsumoto
Keyword(s):  
High Frequency ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Glucosephosphate Isomerase ◽  
Electrophoretic Mobilities ◽  
Starch Gel ◽  
Allelic Isozymes ◽  
F2 Generation ◽  
Species Specific ◽  
Green Sunfish

ABSTRACT The purpose of the present investigation is to determine whether the two duplicated glucosephosphate isomerase (EC 5.3.1.9) loci Gpi-A and Gpi-B reside on the same chromosome in teleostean fishes. Interspecific sunfish hybrids were employed for the cross because of the different species-specific electrophoretic mobilities of the allelic isozymes at each GPI locus and because of their genomic compatibility. F1 sunfish hybrids, formed from a male warmouth (Lepomis gulosus) × female green sunfish (L. cyanellus) cross, were mated to form the F2 generation. The number of each of the nine different isozyme phenotypes, revealed by starch gel electrophoresis, was determined using 256 F2 individuals. The high frequency of recombinant phenotypes in the F2 generation indicated that the two GPI loci are not linked. An excess of F2 individuals heterozygous at both loci was observed and is interpreted as being caused by heterosis. The absence of linkage for the homologous loci encoding GPI subunits and for other multilocus isozyme systems is consistent with the postulate that the genomes of present-day vertebrates arose through one or more polyploidization events early in vertebrate evolution.

scholarly journals Studies on Reduced Wool III. Starch-Gel Electrophoresis of Extracted Wool Proteins

1964 ◽  
Vol 17 (1) ◽  
pp. 277 ◽  
Author(s):  
EOP Thompson ◽  
IJ O'donnell
Keyword(s):  
Gel Electrophoresis ◽  
Moving Boundary ◽  
Electrophoretic Pattern ◽  
Deae Cellulose ◽  
Protein Fractions ◽  
Single Peak ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Wool Proteins

Starch-gel electrophoresis in 8M urea has been used to demonstrate the presence of many components in wool protein fractions extracted from reduced and alkylated wool. All preparations of low-sulphur wool proteins gave mUltiple bands on starch gel in 8M urea even though some of these had previously been fractionated to give a single peak using moving-boundary electrophoresis in the absence of 8M urea. The heterogeneity suggested by these results is in Rccord with that found by chromatography of the proteins on DEAE-cellulose in buffers containing 8M urea. With stepwise elution from DEAE-cellulose it is possible to obtain fractions responsible for various sections of the starch-gel electrophoretic pattern.

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.

FURTHER STUDIES OF CHANGES IN PLASMA PROTEINS IN AVIAN ERYTHROBLASTOSIS: II. INVOLVEMENT OF α-LIPOPROTEIN

1965 ◽  
Vol 43 (10) ◽  
pp. 1667-1675 ◽  
Author(s):  
Mohendra Merriman ◽  
C. le Q. Darcel
Keyword(s):  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Electrophoretic Pattern ◽  
Starch Gel Electrophoresis ◽  
Normal Plasma ◽  
Starch Gel ◽  
Protein Components

Earlier studies with paper and starch gel electrophoresis of plasma from birds with erythroblastosis indicated an alteration in the mobility of one of its protein components. This protein has now been shown to be α-lipoprotein. Efforts have been made to simulate leukemic changes experimentally in normal plasma. Of all the treatments and materials tried, only incubation with turpentine and pinene compounds produced alterations in the electrophoretic pattern closely resembling those in leukemia.

scholarly journals Isolation and characterization of α-1-antitrypsin from rhesus-monkey serum

1976 ◽  
Vol 159 (1) ◽  
pp. 95-104 ◽  
Author(s):  
R W Berninger ◽  
R K Mathis
Keyword(s):  
Rhesus Monkey ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Electrophoretic Pattern ◽  
Deae Cellulose ◽  
Starch Gel Electrophoresis ◽  
Human Phenotype ◽  
Isolation And Characterization ◽  
Starch Gel ◽  
Alpha 1 Antitrypsin

A simple, relatively gentle, procedure for isolation of rhesus-monkey alpha-1-antitrypsis from serum is described. The method consists of chromatographic separation of the fraction precipitated by 50-75%-satd. (NH4)2SO4 from pooled monkey serum on DEAE-cellulose followed by affinity chromatography on Sepharose-bound concanavalin A. Approx. 30% of the trypsin-inhibitory activity present in the original serum was recovered when alpha-1-antitrypsin was reconstituted with physiological saline (0.85% NaCl). Pure alpha-1-antitrypsin exhibitied a single band on sodium docecyl sulphate/polyacrylamide-gel electrophoresis, with an estimated mol.wt. of 60000 and four bands in acid/starch-gel electrophoresis. The acid/starch-gel-electrophoretic pattern and mobility of isolated material were identical with those of the alpha-1-antitrypsin bands in the original serum sample. The most rapdily migrating bands resembled the pattern and mobility for the normal human phenotype PiM in 28 monkeys. A starch strip from the acid/starch-gel-electrophoresis as the origin for antigen-antibody electrophoresis was used to examine alpha-1-antitrypsin for microheterogeneity; no evidence for microheterogeneity was observed in samples from 18 monkeys. In addition, isolated alpha-1-antitrypsin exhibited a single arc when subjected to immunoelectrophoresis. Amino acid and carbohydrate compositions of isolated monkey alpha-1-antitrypsin were similar to those of human alpha-1-antitrypsin.

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.

Sign in / Sign up

Export Citation Format

Share Document