Title : Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N.

Pub. Date : 1988 Aug 15

PMID : 2902847






5 Functional Relationships(s)
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1 The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. 2,6-dichloro-4-nitrophenol alanyl aminopeptidase, membrane Sus scrofa
2 The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. 2,6-dichloro-4-nitrophenol alanyl aminopeptidase, membrane Sus scrofa
3 At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. 2,6-dichloro-4-nitrophenol alanyl aminopeptidase, membrane Sus scrofa
4 At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. Sulfates alanyl aminopeptidase, membrane Sus scrofa
5 In labelling experiments with [35S]methionine from 0.5 to 5 h, DCNP was tested for its possible influence on synthesis, processing and microvillar expression of aminopeptidase N, but no effect on any of these parameters could be detected. 2,6-dichloro-4-nitrophenol alanyl aminopeptidase, membrane Sus scrofa