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.

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.

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.

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.

A Study of Detergent Pollution By Molecular Methods: Starch Gel Electrophoresis of a Variety of Enzymes and Other Proteins

1967 ◽  
Vol 47 (3) ◽  
pp. 659-675 ◽  
Author(s):  
Clyde Manwell ◽  
C. M. Ann Baker
Keyword(s):  
Gel Electrophoresis ◽  
Plasma Proteins ◽  
Marine Species ◽  
Serum Lipoprotein ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Irreversible Effect ◽  
General Opinion

Tissues from a number of marine species were treated with a variety of solutions, including 1% of the major ‘detergent’ (B.P. 1002) used in attempting to disperse the oil from the ‘Torrey Canyon’ and 1% of each of the three major constituents of B.P. 1002, two of which are non-ionic surfactants.The extracts were submitted to vertical starch-gel electrophoresis in order to measure both the effect of the detergent in facilitating the breakdown of cellular structure (extractability), and the irreversible effect on activation or inhibition of various enzymes and other proteins.The proteins studied include a variety of NAD- and NADP-linked dehydrogenases, esterases, blood and nerve haemoglobins, plasma proteins, egg white and yolk proteins, and r-phycoerythrin.The results confirm the general opinion that detergents increase the extractability of proteins from cells. In particular lipoprotein systems are altered, e.g. ‘fast’ serum lipoprotein in fishes (and other vertebrates). Other effects are also observed, e.g. sole but not turbot haemoglobin is rendered relatively insoluble, probably because the detergent stabilizes haemoglobin binding to other components in the erythrocyte. Certain enzymes, e.g. some esterases and amylases, are activated—a not surprising observation. However, a few enzymes are altered in electrophoretic mobility or in activity in a way that one might not expect, e.g. bass Morone labrax lactate dehydrogenase.The results indicate that ‘oil-spill’ detergents and their constituent surfactants are biochemically quite powerful agents. It is too early to attempt to correlate in vitro and in vivo observations but there is an indication that starch-gel electrophoresis provides a useful supplement to more conventional methods used in the studies on complex pollution problems.

Bovine Platelet Proteins II. Purification of Platelet Fibrinogen

1969 ◽  
Vol 21 (03) ◽  
pp. 419-427 ◽  
Author(s):  
N. O Solum ◽  
S Łopaciuk
Keyword(s):  
Analytical Ultracentrifugation ◽  
Insoluble Fraction ◽  
Disc Electrophoresis ◽  
Plasma Fibrinogen ◽  
Starch Gel Electrophoresis ◽  
Freezing And Thawing ◽  
Insoluble Material ◽  
High Resolution Power ◽  
Starch Gel ◽  
Platelet Proteins

Summary1. Platelet fibrinogen has been purified from washed bovine platelets. The procedure was based on the methods for purification of plasma fibrinogen by fractionated precipitations and extractions with ethanol and glycine below 0°, and precipitation of proteins by dimethylformamide at 0°.2. The platelet extract obtained by freezing and thawing of the cells, freed from insoluble material by centrifugation at 23,000 x g for 30 min, contained 0.22 ±0.003mg fibrinogen per 109 platelets. Total protein of this fraction was 0.77 ±0.08 mg per 109 platelets whereas that of the insoluble fraction was 0.79 ±0.09 mg per 109 platelets.3. The most purified platelet fibrinogen fraction contained 91-98% of the protein in a thrombin-clottable state. The yield was approx. 20%. It showed homogeneity in analytical ultracentrifugation, in immunoelectrophoresis using an antiserum produced by immunization of rabbits against platelet extract, and in starch gel electrophoresis using a discontinuous system of Tris HCl and borate buffers offering a high resolution power towards the platelet proteins. Polyacrylamide disc electrophoresis revealed two to three faint lines behind the main fibrinogen line. At least one such line was also observed with purified plasma fibrinogen.

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.

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