Organization of Krebs tricarboxylic acid cycle enzymes.
Binding of enzymes of the Krebs TCA cycle to biological membranes was characterized with respect to intracellular location, susceptibility to various chemical and physical treatments, and extractability as a macromolecular component of the mitochondrial inner membrane. It was shown that citrate synthase and malate dehydrogenase bind to the inner membrane in an ionic strength-sensitive, saturable, and specific manner to a relatively thermostabile component manifested on the inner (matrix) surface of the inner membrane of the mitochondrion. From these data several arguments in support of the physiological applicability of these processes were deduced, and the question of whether these two enzymes bind to the same or different membrane components was considered. Also, experiments preliminary to purification of the citrate synthase binding component were presented.
D000818:Animals; D002499:Centrifugation, Density Gradient; D002950:Citrate (si)-Synthase / Q000378:metabolism; D002952:Citric Acid Cycle; D006358:Hot Temperature; D007425:Intracellular Membranes / Q000201:enzymology; D008291:Malate Dehydrogenase / Q000378:metabolism; D008930:Mitochondria, Liver / Q000201:enzymology*; D009994:Osmolar Concentration; D011092:Polyethylene Glycols / Q000494:pharmacology; D051381:Rats; D013552:Swine
D011092:Polyethylene Glycols; D008291:Malate Dehydrogenase; D002950:Citrate (si)-Synthase