Abstract
1. 1. The solubilization of LDH 5 from chicken muscle particulates depended on pH and concentration of NADH and particulates. There was some solubilization by NAD +, but it was less than that of NADH. 2. 2. LDH 3 was more easily solubilized than LDH 5; LDH 1 was not bound under any of the conditions studied. 3. 3. Solubilization of LDH 5 from mitochondria and microsomes was similar to that from whole muscle particulates except that maximal solubilization was less with these subcellular fractions. 4. 4. LDH 5 bound equally well to mitochondrial structural protein or a structural proteinphospholipid complex.
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