OLIGOMERIC STATE AND MEMBRANE-BINDING BEHAVIOR OF CREATINE-KINASE ISOENZYMES - IMPLICATIONS FOR CELLULAR FUNCTION AND MITOCHONDRIAL STRUCTURE

The membrane binding properties of cytosolic and mitochondrial creatin e kinase isoenzymes are reviewed in this article. Differences between both dimeric and octameric mitochondrial creatine kinase (Mi-CK) attac hed to membranes and the unbound form are elaborated with respect to p ossible biological function. The formation of crystalline mitochondria l inclusions under pathological conditions and its possible origin in the membrane attachment capabilities of Mi-CK are discussed. Finally, the implications of these results on mitochondrial energy transduction and structure are presented.