A Comparison of the Plasma Proteins of C3H Strain Mice, found by Cellulose-Acetate and Starch-Gel Electrophoresis

Nature ◽  
1963 ◽  
Vol 197 (4864) ◽  
pp. 288-289 ◽  
Author(s):  
E. J. DUKE
Keyword(s):  
Cellulose Acetate ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Starch Gel Electrophoresis ◽  
Starch Gel

scholarly journals Clonal variation within a mucosal isolate derived from a patient with Leishmania (Viannia) braziliensis infection

1991 ◽  
Vol 33 (5) ◽  
pp. 343-350 ◽  
Author(s):  
César Augusto Cuba-Cuba ◽  
David Evans ◽  
Ana de Cassia Rosa ◽  
Philip Davis Marsden
Keyword(s):  
Monoclonal Antibodies ◽  
Cellulose Acetate ◽  
Phenotypic Variation ◽  
Gel Electrophoresis ◽  
Clonal Variation ◽  
Starch Gel Electrophoresis ◽  
Mucosal Leishmaniasis ◽  
Starch Gel

Three isolates over 5 years from a patient with persistent relapsing mucosal leishmaniasis due to Leishmania (Viannia) braziliensis and 7 clones from one of these isolates were studied by zymodemes and scrodemes analysis. Results showed evidences of clonal phenotypic variation. Eight isoenzymes markers demonstrated clear differences on Cellulose Acetate (CA) and thin starch gel electrophoresis. Also a panel of specific monoclonal antibodies showed such differences. Our observations provide additional evidence that Leishmania (Viannia) braziliensis is composed by subpopulations of parasites with peculiar biochemical and antigenic characteristics.

Inter-Species Relationships Within the Genus Oncorhynchus Based on Biochemical Systematics

1966 ◽  
Vol 23 (1) ◽  
pp. 101-107 ◽  
Author(s):  
H. Tsuyuki ◽  
E. Roberts
Keyword(s):  
Phylogenetic Relationships ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Disc Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Species Relationships ◽  
Oncorhynchus Masou ◽  
Starch Gel ◽  
Specific Muscle ◽  
Species Specific

The species specific muscle myogens of Salmo gairdnerii, Oncorhynchus masou, O. masou ishikawae, O. kisutch, O. tshawytscha, O. keta, O. nerka, and O. gorbuscha are compared by starch gel electrophoresis. Plasma proteins of these same species are also examined by polyacrylamide disc electrophoresis. The range of usefulness of muscle myogens in species identification, and equally significantly, their value in establishing phylogenetic relationships of closely related groups, as the genus Oncorhynchus, are discussed. The myogen patterns of O. keta and O. gorbuscha from the Asiatic and North American coasts were found to be identical, further supporting the concept of absolute species specificity of these patterns.

CONFIRMATION OF PLASMA PROTEIN CHANGES IN AVIAN ERYTHROBLASTOSIS

1964 ◽  
Vol 42 (2) ◽  
pp. 293-297 ◽  
Author(s):  
M. Merriman ◽  
C. le Q. Darcel
Keyword(s):  
Plasma Protein ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Starch Gel Electrophoresis ◽  
Starch Gel

Alterations of the plasma proteins have been previously demonstrated in avian erythroblastosis by paper and now by starch gel electrophoresis. With the latter technique, eight protein zones are recognized in normal plasmas. Heparin contributes an additional non-staining zone. In leukemic plasmas two more zones occur while another zone shows significant retardation.Heparin is not responsible for these changes because they are also observed in oxalated plasmas, but there is evidence of increased binding of heparin in leukemic plasma.

Comparative Zone Electropherograms of Muscle Myogens and Blood Proteins of Adult and Ammocoete Lamprey

1967 ◽  
Vol 24 (6) ◽  
pp. 1269-1273 ◽  
Author(s):  
J. F. Uthe ◽  
H. Tsuyuki
Keyword(s):  
Great Lakes ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Disc Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Blood Proteins ◽  
Adult Form ◽  
Starch Gel

Polyacrylamide disc electrophoresis of plasma proteins and starch-gel electrophoresis of hemoglobins and muscle myogens of adult and ammocoete forms of three species of Great Lakes lamprey were carried out. Blood proteins were shown to undergo marked changes upon transformation of the ammocoete into the adult form. Muscle myogen did not undergo any change during transformation. The muscle myogen electropherograms of Ichthyomyzon unicuspis and Lampetra lamottei were found to be the same.

Human Prothrombin

1970 ◽  
Vol 24 (03/04) ◽  
pp. 311-324 ◽  
Author(s):  
Th. R Derleth ◽  
J. A Penner
Keyword(s):  
Cellulose Acetate ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Ix ◽  
Factor Vii ◽  
Starch Gel Electrophoresis ◽  
Multiple Protein ◽  
Starch Gel

SummaryA method is presented for the chromatographic separation of human prothrombin from variable volumes of plasma. The procedure is simple, consisting of chromatography on ECTEOLA which provides a potent product containing factor IX and X activity sufficient for therapeutic use. Additional chromatography on DEAE or Sephadex G200 will produce a prothrombin of high specific activity which appears homogeneous by ultracentrifugation and electrophoresis on cellulose acetate, although multiple protein fractions can be identified on starch gel electrophoresis.Human prothrombin prepared by this method migrates as an alpha 2-globulin and does not appear to be altered electrophoretically or antigenically from its original state in the plasma. The characteristics of human prothrombin obtained from patients with deficiencies of factor VII or IX do not differ from normal.

scholarly journals Genetics of plasma transferrins in the mouse

1960 ◽  
Vol 1 (3) ◽  
pp. 431-438 ◽  
Author(s):  
B. L. Cohen
Keyword(s):  
Gel Electrophoresis ◽  
Molecular Basis ◽  
Plasma Proteins ◽  
Inbred Strains ◽  
The Other ◽  
Starch Gel Electrophoresis ◽  
Widespread Distribution ◽  
Agouti Locus ◽  
Inbred Strains Of Mice ◽  
Starch Gel

1. The plasma proteins of six inbred strains of mice have been studied, using starch-gel electrophoresis.2. The existence of two alternative plasma transferrin (β-globulin) phenotypes has been demonstrated. Five of the strains have one of these and one strain has the other. Each of the two transferrin patterns comprises three (or possibly only two) electrophoretic bands. The two patterns differ in all of these bands.3. The two transferrin types recognized are determined by a pair of allelic, autosomal genes (designated TrfA and TrfB). The TrfA phenotype (CBA strain) is determined by the genotype TrfA/TrfA, and the TrfB phenotype (A, C57BL, JU, KL, RIII strains) by the genotype TrfB/TrfB. The phenotype TrfAB, of the heterozygote (genotype TrfA/TrfB), is distinguishable and shows four (or possibly only three) bands. In this way it closely resembles a mixture of equal parts of TrfA and TrfB plasma.4. No linkage was detected between the Trf locus and sex, the agouti locus or the haemoglobin locus.5. The possible molecular basis of the action of the transferrin alleles in the mouse, and the widespread distribution in mammals of polymorphism involving the transferrins, are discussed.

FURTHER STUDIES OF CHANGES IN PLASMA PROTEINS IN AVIAN ERYTHROBLASTOSIS: I. TWO-DIMENSIONAL STARCH GEL ELECTROPHORESIS

1965 ◽  
Vol 43 (10) ◽  
pp. 1661-1665 ◽  
Author(s):  
Mohendra Merriman
Keyword(s):  
Plasma Protein ◽  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Starch Gel

Plasma protein changes in avian erythroblastosis previously studied with paper and starch gel electrophoresis have now been examined with a two-dimensional technique combining the two methods. The differences affect chiefly one zone which migrates in the α-globulin region.

scholarly journals Further studies on the inheritance of lymph proteins in Drosophila melanogaster

1966 ◽  
Vol 7 (3) ◽  
pp. 287-294 ◽  
Author(s):  
E. J. Duke
Keyword(s):  
Drosophila Melanogaster ◽  
Cellulose Acetate ◽  
Gel Electrophoresis ◽  
Protein Fraction ◽  
Autosomal Gene ◽  
Single Pair ◽  
Starch Gel Electrophoresis ◽  
Dominant Allele ◽  
The Third ◽  
Starch Gel

The inheritance of three protein fractions of third instar larval lymph in Drosophila melanogaster as detected by starch gel electrophoresis is described. Each of the three is governed by a single autosomal gene. In two, the dominant allele determines presence, and the recessive absence of the respective fraction. The third protein fraction is governed by a single pair of co-dominant alleles.Comparison of the starch-gel pattern to that obtained on cellulose acetate and on polyacrylamide gel fails to show definite sub-fractionation of those protein bands of which the inheritance has been studied.

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.

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