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Isozymes of glyceraldehyde‐3‐phosphate dehydrogenase in man and other mammals
Author(s) -
EDWARDS YVONNE H.,
CLARK PEGGY,
HARRIS HARRY
Publication year - 1976
Publication title -
annals of human genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.537
H-Index - 77
eISSN - 1469-1809
pISSN - 0003-4800
DOI - 10.1111/j.1469-1809.1976.tb00165.x
Subject(s) - isozyme , glyceraldehyde 3 phosphate dehydrogenase , dehydrogenase , biochemistry , glyceraldehyde , locus (genetics) , biology , enzyme , red cell , microbiology and biotechnology , chemistry , gene , computer security , computer science
Multiple electrophoretically distinct forms of glyceraldehyde-3-phosphate dehydrogenase have been observed in human and other mammalian tissues. The human isozymes appear to have essentially the same structural and kinetic properties. An apparent correlation between red-cell age and the relative intensities of the isozymes supports the idea that the isozymes arise as a result of post-translational modification of the polypeptide chain. The possibility that a second locus is involved in the determination of these isozymes is discussed.