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By G. Rickey Welch

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It is clear therefore that good physical and chemical evidence exists that specific complexes of metabolically sequential enzymes of the Krebs TCA cycle and TCA cycle-associated enzymes are formed. The results of these studies on protein interactions are summarized in Fig. 3. Not all of the possible relevant interactions have been studied as yet but the data thus far presented I think argue strongly for the existence of such complexes. 3. Matrix Protein Interactions as Studied by Cross-Linking Techniques Cross-linking techniques have been used to stabilize the weak interactions of proteins in situ with the aim of studying the possible subcompartmentation of different proteins in cells and cellular organelles (Peters and Richards, 1977).

These calculations on diffusion rates, however, are dependent on a number of assumptions. Using the simple Einstein mean square equation, Ä2 (distance) = 2D (diffusion coefficient) Äß(time), Ä2 = mean square of AX (distance). In a dimensional analysis this would be cm2 = cm2 s - 1 s. 5 x 1(Ã3 s. The turnover number of enzymes varies from 102 to 106 s"1. Citrate synthase is 104 min -1 or about 250 s _1 . So that in this case it would appear at first that diffusion time would be meaningful. The assumptions were one substrate molecule, one enzyme molecule, pure water, and an unhindered path for mean square calculation, and it was also assumed that the molecules will meet in a productive encounter.

Previous studies using differential centrifugation had indicated that AAT wasfirmlybound to the inner mitochondrial membrane. The enzymatic reaction product could be demonstrated in the cristae of mitochondria only when the mitochondria had beenfixedin situ. When mitochondria were isolated and fixed, then no GOT activity could be detected histochemically or biochemically. e. Carbamoyl Phosphate Synthethase. The first published report using labeled antibodies for the localization of a mitochondrial matrix enzyme was for carbamoyl phosphate synthetase.

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