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Intracellular Localization of Hepatic Propionyl‐CoA Carboxylase and Methylmalonyl‐CoA Mutase in Humans and Normal and Vitamin B 12 Deficient Rats
Author(s) -
Frenkel Eugene P.,
Kitchens Richard L.
Publication year - 1975
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1975.tb00885.x
Subject(s) - mutase , intracellular , pyruvate carboxylase , biochemistry , chemistry , endocrinology , medicine , biology , enzyme
S ummary . The intracellular localization of the enzymes in the vitamin B 12 dependent pathway which involves the oxidation of propionate was studied in rat liver obtained from normal and vitamin B 12 deficient rats as well as from man. The subcellular site of propionyl CoA carboxylase and the vitamin B 12 dependent‐methylmalonyl CoA mutase were determined. All of the activity of these two enzymes was demonstrated to be in the mitochondria and those enzymes were shown to be loosely bound to the inner membrane‐matrix portion of the mitochondria. Vitamin B 12 deficiency did not alter the subcellular localization. Finally, a rapid enzymatic assay for methylmalonyl‐CoA mutase was described.