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|Title:||ENDO-OLIGOPEPTIDASE-A, A PUTATIVE ENKEPHALIN-GENERATING ENZYME, in the VERTEBRATE RETINA|
|Authors:||Ferro, E. S.|
Hamassaki, D. E.
Universidade Federal de São Paulo (UNIFESP)
São Paulo STATE UNIV
|Citation:||Journal of Neurochemistry. Philadelphia: Lippincott-raven Publ, v. 57, n. 5, p. 1643-1649, 1991.|
|Abstract:||Endo-oligopeptidase A, EC 22.214.171.124, converts small enkephalin-containing peptides into the corresponding enkephalins in vitro. We investigated the presence of endooligopeptidase A in the retina and its possible colocalization with enkephalins in retinal neurons. the specific activity of endo-oligopeptidase A found in pigeon retinae (30.3 +/- 7.3 mU/mg, mean +/- standard deviation) was four times higher than in rabbit retinae (7.0 +/- 1.1 mU/mg). the enzyme activity was not modified by EDTA, but it was enhanced by dithiothreitol and inhibited by zinc and 5,5'-dithiobis(2-nitrobenzoic acid). Immunohistochemical experiments with a purified antiserum against rabbit endo-oligopeptidase A revealed labeled neurons in both the inner nuclear layer and the ganglion cell layer of pigeon and rabbit retinae. Double-labeling immunofluorescence experiments demonstrated that about 90% of neurons containing endo-oligopeptidase A-like immunoreactivity also contained [Leu5]-enkephalin-like immunoreactivity. These colocalization results may represent an important step toward the demonstration of the possible involvement of endo-oligopeptidase A in enkephalin generation in vivo.|
|Appears in Collections:||Em verificação - Geral|
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