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E S VESELL

Publications and source records attributed to E S VESELL.

At least 19 recordsLinked to original sources
PubMed1965

POLYMORPHISM OF HUMAN LACTATE DEHYDROGENASE ISOZYMES.

Of 1200 individuals screened, four had variant erythrocyte lactate dehydrogenases. Three of these, identical electrophoretically to the Mem-1 described by Kraus and Neely, were heterozygous variants involving the a-locus. The fourth, involving the b-locus, appears to be the first example in man of a homozygous variant.

Black People↗
PubMed1962

Comparative studies of the isozymes of lactic dehydrogenase in rabbit and man. Observations during development and in tissue culture.

During development of rabbit tissues, characteristic sequential alterations in the LDH isozyme pattern occur, and consist for liver and muscle in loss of the most rapidly migrating anodal bands, and increased activity in the cathodal bands and slower migrating anodal bands. In heart the reverse changes were observed. Comparison of the isozyme patterns observed in various fetal and adult human tissues suggests that these same sequential alterations probably occur. A species-specific isozyme pattern is obtained in long term culture of rabbit, chick, and human cells. The alterations in tissue culture are characterized by a gradual redistribution of total LDH activity in which there is decreased intensity of rapidly migrating anodal bands. These sequential alterations are independent of the organ of origin. The number of bands observed in the starch gel is partly dependent upon the total activities applied. Isozymes may provide a convenient method for determining the species of origin of cell lines in common use and for investigating the effects of various alterations in the in vitro environment on cells grown in tissue culture.

Animals↗
PubMed1962

Variations in the lactic dehydrogenase of vertebrate erythrocytes.

Erythrocytes from representatives of the 5 classes of vertebrates revealed a marked species variation in the number of LDH isozymes, in the distribution of the total LDH activity among these isozymes, and in their electrophoretic mobilities. Starch gel electrophoresis of hemolysates followed by direct histochemical demonstration of LDH activity with nitro blue tetrazolium as dye and phenazine methosulfate as electron transporter showed that closely related species exhibited similar LDH patterns. The rhesus monkey had LDH isozymes of similar pattern to those of human hemolysate but slightly slower in electrophoretic mobility. The goat and sheep each had 1 band of LDH activity in their erythrocytes of identical electrophoretic mobility, whereas the single band in steer hemolysate migrated slightly faster. The 5 bands of chicken hemolysate were quite similar in pattern to the 5 bands of duck hemolysate but migrated slightly faster and exhibited a different distribution of the total LDH activity. The 2 species of snake each had 1 band of LDH activity with identical mobility. Staining occurred with the levorotatory form of the substrate and not with the dextrorotatory form. Examination of more than 380 human hemolysates failed to reveal any differences among individuals in the main LDH bands. The genetic basis for the species differences in erythrocyte lactic dehydrogenases is discussed.

Animals↗