Aminopeptidase is uniformly distributed in the proximal tubules of pig kidneys, suggesting all sections function equivalently in peptide hydrolysis.
Uniform distribution implies equivalent peptide hydrolysis along pig proximal tubules; leaves open human relevance pending further study.
The concentration of aminopeptidase in cross-sections in proximal tubules of pig kidney was investigated with a specific fluorescent antibody technique and a specific histochemical technique. The concentration was found to be independent of the diameter of the tubule and of the depth of the cortex. Four-micron segments of proximal tubules contained approximately l0 4 molecules of aminopeptidase/µ 2 , which is adequate for a rapid hydrolysis of peptides, even in very small concentrations, such as angiotensin II at 10 5 of the physiologic serum concentration. The findings suggest that with regard to this enzyme all sections of the proximal tubule function equivalently.
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Wachsmuth et al. (1973) studied this question.
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