Abstract: An antiserum generated to the soluble form of the rat brain puromycin‐sensitive enkephalin‐degrading amino‐peptidase was used to determine the tissue distribution of the soluble and membrane‐associated forms of this enzyme. All tissues examined contained significant levels of the soluble enzyme form, with this enzyme accounting for >90% of the arylamidase activity in brain, heart, and skeletal muscle. Native gel electrophoresis coupled with activity staining as well as inhibition studies were used to confirm the presence of this enzyme in various tissues. Serum was found not to contain this particular aminopeptidase. In contrast to the results obtained with the soluble enzyme form, brain was the only tissue found to contain the membrane‐associated enzyme form. Although all tissues contained membrane‐associated aminopeptidase activity only the brain enzyme could be maintained in solution in the absence of detergent. In addition, the brain membrane‐associated enzyme could be distinguished from the membrane‐associated aminopeptidase activity in other tissues on the basis of its sensitivity to inhibition by puromycin.
|Number of pages||8|
|Journal||Journal of Neurochemistry|
|State||Published - Nov 1988|
- Puromycin‐sensitive aminopeptidases
- Tissue distribution
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience