pPure rat intestinal maltase/glucoamylase was partially inactivated in 1% sodium dodecyl sulphage by heating at 40–70 degree C for 5 min at pH 7.5, or by lowering the pH to 5.4–6.6 at 24 degree C. When partially active preparations were electrophoresed in the presence of sodium dodecyl sulphate, a complicated protein band pattern of incompletely dissociated fragments of the enzyme was observed. Complete dissociation of the enzyme in sodium dodecyl sulphate, induced by boiling or by pH values below 5.4, was accompanied by total loss of enzyme activity and simplification of the protein pattern to five major species. Although the original enzyme band was absent from some partially dissociated preparations, enzyme activity was present and was associated with several transient protein bands on the gels. Maltase and alpha-glucosidase activities were detected in these bands, but glucoamylase activity was absent./p
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