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Human mitochondrial glycerol phosphate dehydrogenase (GPD M ) isozymes
Author(s) -
SHAW M. A.,
EDWARDS Y. H.,
HOPKINSON D. A.
Publication year - 1982
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.1469-1809.1982.tb00690.x
Subject(s) - isozyme , dehydrogenase , glycerol 3 phosphate dehydrogenase , biochemistry , biology , chemistry , genetics , enzyme
Summary1 A hydrophobic/phospholipid electrophoretic system has been devised which makes possible the analysis of human mitochondrial glycerol phosphate dehydrogenase (E.C. 1.1.99.5, GPD M . 2 GPD M has a wide tissue distribution in both adult and foetal life and is active in cultured lymphoblastoid cells and fibroblasts but is absent from red cells. 3 The solubilization procedure does not significantly alter the kinetic properties of the enzyme (K m α‐glycerophosphate = 0.04‐0.07 m , K m PMS = 0.19‐0.35 m m ) but the soluble form is less thermostable. 4 Comparisons of physicochemical characteristics, tissue distribution and coenzyme requirement point to a separate genetic determination and low level of evolutionary relatedness between GPD M and its cytosolic counterpart GPD s .