Comparison of soluble and membrane-bound pyroglutamyl peptidase I activities in rat brain tissues in the presence of detergents.

Abstract:

:Pyroglutamyl peptidase I activity from soluble and membrane-bound fractions of rat brain homogenates is inhibited by the presence of sodium deoxycholate but not by triton X-100. Biobeads SM2, a polystyrene adsorbent reported to be useful in removing detergents from aqueous solutions, inhibits enzymatic activity in both fractions regardless of the presence of these detergents, probably because of partial adsorption of the enzyme by the polymeric microspheres. These effects seem to be enzyme-specific since other aminopeptidase activities are not affected by detergents or biobeads. The results suggest that soluble and membrane-bound forms of the enzyme represent the same protein in two different cell compartments.

journal_name

Neuropeptides

journal_title

Neuropeptides

authors

Alba F,Arenas JC,Lopez MA

doi

10.1016/0143-4179(95)90092-6

subject

Has Abstract

pub_date

1995-08-01 00:00:00

pages

103-7

issue

2

eissn

0143-4179

issn

1532-2785

pii

0143-4179(95)90092-6

journal_volume

29

pub_type

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