Alanine aminopeptidase (particle-bound aminopeptidase, EC 3.4.11.2)
isolated in a highly purified state from human liver, kidney, and pancreas were investigated
with regard to their different electrophoretic mobilities. While the molecular weights are
identical, different isoelectric points were found. The results of carbohydrate analysis
point to N-acetylneuraminic acid as the main factor that causes the differences in electrophoretic
behaviour of the alanine aminopeptidases investigated.
Using agarose gel electrophoresis, a faster moving alanine aminopeptidase
(EC 3.4.11.2) has been demonstrated in the urine from cases of Fanconi syndrome, endemic
(Balkan) nephropathy and advanced renal insufficiency. The enzyme was partially purified
and its properties (isoelectric point, molecular weight, substrate specificity, influence of metal
ions, Michaelis constant, antigenic behavior) were compared with those of normal kidney
alanine aminopeptidase. Isoelectric points and antigenic properties are identical, but the
molecular weights differ by a factor of about 2. Therefore, the greater electrophoretic mobility
is due to the smaller size of the atypical enzyme.
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