Abstract
Methods of isolating NAD-glucohydrolase from the microsomal fraction of the heart were tested. NAD-glucohydrolase was found to pass into the soluble state under the influence of phospholipase A, Triton X-100, and Na cholate. NAD-glucohydrolase from heart muscle has unique properties: it is reversibly denatured by 6 M urea but is not inactivated by its own substrate (NAD) at pH 8.0; reversible denaturation by urea correlates for NAD-glucohydrolases isolated from other sources as a rule with inactivation of the enzyme in the presence of NAD at pH 8.0.
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Boriskina, G.M., Tseitlin, L.A. Solubilization and some properties of NAD-glucohydrolase isolated from rabbit heart. Bull Exp Biol Med 79, 33–35 (1975). https://doi.org/10.1007/BF00805498
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DOI: https://doi.org/10.1007/BF00805498