SUMMARY—The distribution of lactate dehydrogenase (LDH) in chicken breast muscle was studied by preparing subcellular fractions by homogenization and differential centrifugation under conditions known to cause the enzyme to be associated with the particulate structures. The LDH was widely distributed among the subcellular fractions with the outer cell membrane and the mitochondrion having especially high activities associated with them.A 4‐hr aging period of the whole, excised muscle had only a minor effect on the subcellular distribution of the enzyme. The major change in aged muscle was an increase of enzymic activity in the soluble, supernatant fractions. Although certain possible artifacts have been ruled out, it is not completely certain that the particle‐associated LDH is a true reflection of the situationin vivo.There is at least, however, a reproducible pattern to the binding of LDH to the individual subcellular fractions when chicken breast muscle is homogenized under the specified condi
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