Translation of protamine mRNA in a rabbit reticulocyte cell-free system

1977 ◽  
Vol 55 (2) ◽  
pp. 152-158 ◽  
Author(s):  
Lashitew Gedamu ◽  
Gordon H. Dixon
Keyword(s):  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Starch Gel Electrophoresis ◽  
Stages Of Development ◽  
Free System ◽  
Cell Free System ◽  
Polyadenylated Rna ◽  
Starch Gel ◽  
Three Components

Protamine mRNA isolated from the microsomal and postribosomal supernatant fractions of trout testis in poly A(+) (polyadenylated RNA) and poly A(−) (RNA devoid of poly A(+)) forms (Gedamu, L. &Dixon, G.H. (1976)7. Biol. Chem. 251, 1446–1454 and 1455–1463) was translated in the heterologous rabbit reticulocyte cell-free system; the products were shown to be identical in mobility with authentic protamine by polyacrylamide and starch gel electrophoresis. Chromatography, on carboxymethyl cellulose (Whatman CM-52), of the labelled polypeptide products synthesized in this cell-free system in the presence of poly A(+) and poly A(−) mRNA fractions also showed that [14C]arginine was incorporated into all three protamine components resolved in this system, but there was an unequal and variable incorporation of label into the three components with different preparations of mRNA. These results were interpreted as showing that the population of subcomponents of the protamine mRNA coding for the three different protamine polypeptides varied in batches of trout testis at differing stages of development. In addition, the proportion of mRNA components varied between the poly A(+) and poly A(−) editions of the mRNA, and it appeared that the poly A(−) mRNA fraction might represent the product of deadenylation of an earlier population of poly A(+) mRNA.

scholarly journals An Improved Chromatographic Separation of Wheat Gluten Proteins

1965 ◽  
Vol 18 (1) ◽  
pp. 193 ◽  
Author(s):  
CW Wrigley
Keyword(s):  
Column Chromatography ◽  
Chromatographic Separation ◽  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Wheat Gluten ◽  
Starch Gel Electrophoresis ◽  
Gluten Proteins ◽  
Electrophoretic Patterns ◽  
Starch Gel

Gel electrophoresis is at present the best procedure for the analytical fractiona-tion of wheat gluten proteins. Procedures more suitable for preparative studies, such as gel ffitration and column chromatography, have provided only partial fractionation on the basis of gel electrophoresis (Graham 1963; Lee et al. 1963; Wright, Brown, and Bell 1964). Gel electrophoretic patterns of fractions resulting from the carboxymethyl cellulose (CMC) fractionation of Simmonds and Winzor (1961) have been published by Graham (1963) and by Lee et al. (1963). These results showed that each fraction was heterogeneous, with considerable overlapping of electrophoretic bands from neighbouring fractions, and that fractions eluted late in the chromatogram were contaminated because of tailing of earlier fractions. The modification of the Simmonds and Winzor procedure described below results in an improved fractionation of gluten proteins as judged by starch-gel electrophoresis.

HETEROGENEITY OF INSULIN: II. CHROMATOGRAPHY OF INSULIN ON CARBOXYMETHYL CELLULOSE IN UREA CONTAINING BUFFERS

1967 ◽  
Vol 45 (2) ◽  
pp. 221-237 ◽  
Author(s):  
W. W. Dillon ◽  
R. G. Romans
Keyword(s):  
Gel Electrophoresis ◽  
Carboxymethyl Cellulose ◽  
Anomalous Behavior ◽  
Starch Gel Electrophoresis ◽  
Electrophoretic Separation ◽  
Minor Components ◽  
Starch Gel ◽  
Starch Gels ◽  
Cellulose Column

Chromatography of insulin, on carboxymethyl (CM) cellulose columns in urea-containing buffers, revealed the presence of at least five components, one major and four minor, in commercial insulin. This fractionation is related to other chromatographic fractionations of insulin and the nature of the minor components is discussed.Insulin which had been incubated in HCl was chromatographed. The behavior of the incubated products on the column showed that two or more amide groups were hydrolyzed simultaneously but at different rates. Because of the anomalous behavior of one of the components, it is postulated that a group other than the amides is also transformed during acid incubation. This component is present in commercial insulin samples.The electrophoretic separation of insulin in urea–starch gels was shown to be due to charge differences on the molecules rather than size differences. Correlation of the components separated on the CM-cellulose column with those separated in the urea–starch gel electrophoresis showed that much smaller charge differences on the molecules are distinguished on the CM-cellulose column than in the gel.

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.

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

Morphological and biochemical systematics of chubs, Nocomis biguttatus and N. micropogon (Pisces: Cyprinidae), in southern Ontario

1981 ◽  
Vol 59 (5) ◽  
pp. 771-775 ◽  
Author(s):  
Moira M. Ferguson ◽  
David L. G. Noakes ◽  
Roy G. Danzmann
Keyword(s):  
Gel Electrophoresis ◽  
Function Analysis ◽  
Morphological Differentiation ◽  
Sexually Dimorphic ◽  
Starch Gel Electrophoresis ◽  
Southern Ontario ◽  
Electrophoretic Mobilities ◽  
Starch Gel ◽  
Respective Species ◽  
Probability Of Misclassification

Examination of 17 presumptive gene loci by starch-gel electrophoresis revealed differential mobilities only at acid phosphatase-1, alcohol dehydrogenase, esterase-1, and phosphoglucomutase between Nocomis biguttatus and N. micropogon. No intraspecific variation was observed for any loci. The genetic identity (I) and genetic distance (D) were 0.874 and 0.134, respectively. The correlation of electrophoretic mobilities and nuptial tubercle pattern in sexually dimorphic males supports the present taxonomic distinction of these species and provides a simple, unambiguous means of identifying any individuals.Stepwise discriminant function analysis of a series of mensural characters was used to compare fish identified as to species by electrophoresis. At best this correctly assigned fish to their respective species in 85.7% of cases, with a probability of misclassification of 0.1335.This study suggests these two are sibling species, based on a comparison of biochemical and morphological differentiation.

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