Rats made diabetes through treatment with streptozotocin showed a relative mean value increase of 8.2-fold in serum alkaline phosphatase (ALP) activity at the 28th day following treatment. On the basis of electrophoretic mobility, this serum ALP was found to consist of principally small intestinal ALP isozyme.
Next, to determine whether the ALP isozyme was of duodenal or ileal origin, the qualitative differences between the purified ALP obtained from tissues of both types were examined in detail. As a result, the serum and ileal ALP matched in terms of specific amino acid inhibition, substrate specificity, and molecular weight, while in examination of the sugar moiety, more of the fraction showing higher affinity to concanavalin A was found with serum ALP than with any of the intestinal ALPs. Serum and intestinal ALPs also differed slightly regarding isoelectric points.
Form the above, it was suggested that the serum ALP of diabetic rats was ileal ALP, translocated into the bloodstream, of which the sugar moiety had been further modified.