Impairment of plasma glycoprotein synthesis in choline deficiency compared with effects of carbon tetrachloride intoxication

1968 ◽  
Vol 46 (3) ◽  
pp. 499-505 ◽  
Author(s):  
Sailen Mookerjea
Keyword(s):  
Carbon Tetrachloride ◽  
Plasma Proteins ◽  
Specific Radioactivity ◽  
Starch Gel Electrophoresis ◽  
Choline Deficiency ◽  
Deficient Diet ◽  
Glycoprotein Synthesis ◽  
Carbon Tetrachloride Intoxication ◽  
Starch Gel ◽  
Plasma Glycoprotein

The incorporation of glucosamine-1-14C into plasma proteins is impaired in rats within 2 days when they are fed a choline-deficient diet. Separation of plasma proteins by starch-gel electrophoresis, and autoradiography of the dried gels, showed four labelled areas (glycoproteins). In choline deficiency there was visual evidence of depletion of radioactivity in the fast α-globulin area, a finding confirmed by the specific radioactivity of proteins eluted from electrophoretic zones of the starch gel. Within 4 h after ingestion of carbon tetrachloride, the synthesis of plasma glycoprotein was reduced by 90% and labelling of all four glycoprotein areas on dried starch gel autoradiograms virtually ceased. The results suggest that the defect in glycoprotein synthesis in carbon tetrachloride intoxication is nonspecific, whereas in choline deficiency the impairment is specific and localized in the fast α-globulin fraction. The results suggest a limiting role of a glycoprotein in the pathway of plasma lipoprotein synthesis.

STUDIES ON THE SYNTHESIS OF PLASMA GLYCOLIPOPROTEIN AND HEPATIC SUB-CELLULAR GLYCOPROTEIN IN EARLY CHOLINE DEFICIENCY

1967 ◽  
Vol 45 (6) ◽  
pp. 825-838 ◽  
Author(s):  
Sailen Mookerjea ◽  
David Jeng ◽  
Judith Black
Keyword(s):  
Liver Microsome ◽  
Specific Radioactivity ◽  
Plasma Lipoproteins ◽  
Residual Fraction ◽  
Choline Deficiency ◽  
Glycoprotein Synthesis ◽  
Limiting Step ◽  
Residual Protein ◽  
Lipoprotein Synthesis ◽  
Smooth Membrane

Impairment of glycoprotein synthesis in trichloroacetic acid insoluble and in residual protein (d > 1.21) fractions of plasma in early choline deficiency has been confirmed. Plasma lipoproteins of d < 1.006, 1.006–1.063, and 1.063–1.21 are also rapidly labelled after intraperitoneal injection of glucosamine-1-14C. In general, there was no difference in specific radioactivity of plasma glycolipoproteins between choline-supplemented rats and rats deprived of choline for 2 days during 180 min of incorporation.Incorporation of glucosamine-1-14C into microsomal glycoprotein is significantly impaired in early choline deficiency. Further sub-microsomal fractionation produced evidence that the site of impairment of glycoprotein synthesis is in the smooth microsome portion. These studies suggest that a decreased synthesis of glycoprotein(s) in liver-microsome smooth membrane and in the plasma residual fraction (d > 1.21) may represent an impairment of 'lipoprotein precursor protein' synthesis in early choline deficiency. An inhibition of this limiting step would possibly impair the rate of plasma lipoprotein synthesis, leading to the development of fatty liver in choline deficiency.

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.

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.

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