TY - JOUR
T1 - Electrophoretic polymorphism of glutathione peroxidase
AU - Beutler, E.
AU - West, C.
AU - Beutler, B.
PY - 1974/10
Y1 - 1974/10
N2 - A method for the detection of glutathione peroxidase after electrophoresis on starch gel has been devised. Blood samples from 780 persons of Caucasian or Negro origin were studied. An electrophoretically fast enzyme, designated as the Thomas variant, was found in 6·4 % of 392 Negro donors and 0·8 % of 388 Caucasian donors. This variant was inherited in an autosomal dominant fashion. A slightly rapid electrophoretic mobility was noted in some cord blood samples and in a father and daughter with a refractory anaemia. Because this variant, designated ‘Musi’ differed so little from the normal variant, it was difficult to further characterize it, but it did not appear that this variant was genetically determined. Glutathione peroxidase from most other tissues had the same electrophoretic mobility as the enzyme from erythrocytes, but the enzyme from cultured human fibroblasts moves more rapidly. Various laboratory animals were found to have electrophoretically distinguishable glutathione peroxidase, but efforts to hybridize hamster enzyme to human enzyme were unsuccessful.
AB - A method for the detection of glutathione peroxidase after electrophoresis on starch gel has been devised. Blood samples from 780 persons of Caucasian or Negro origin were studied. An electrophoretically fast enzyme, designated as the Thomas variant, was found in 6·4 % of 392 Negro donors and 0·8 % of 388 Caucasian donors. This variant was inherited in an autosomal dominant fashion. A slightly rapid electrophoretic mobility was noted in some cord blood samples and in a father and daughter with a refractory anaemia. Because this variant, designated ‘Musi’ differed so little from the normal variant, it was difficult to further characterize it, but it did not appear that this variant was genetically determined. Glutathione peroxidase from most other tissues had the same electrophoretic mobility as the enzyme from erythrocytes, but the enzyme from cultured human fibroblasts moves more rapidly. Various laboratory animals were found to have electrophoretically distinguishable glutathione peroxidase, but efforts to hybridize hamster enzyme to human enzyme were unsuccessful.
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U2 - 10.1111/j.1469-1809.1974.tb01947.x
DO - 10.1111/j.1469-1809.1974.tb01947.x
M3 - Article
C2 - 4467780
AN - SCOPUS:0016283485
SN - 0003-4800
VL - 38
SP - 163
EP - 169
JO - Annals of Human Genetics
JF - Annals of Human Genetics
IS - 2
ER -