Methionyl aminopeptidase from rat liver: distribution of the membrane-bound subcellular enzyme

Methionyl aminopeptidase from rat liver: distribution of the membrane-bound subcellular enzyme

Author Termignoni, Carlos Google Scholar
Freitas Junior, Jose Olavo de Autor UNIFESP Google Scholar
Guimarães, Jorge Almeida Google Scholar
Institution Universidade Federal do Rio de Janeiro (UFRJ)
UNIV FED RIO GRANDE SUL
Universidade Federal de São Paulo (UNIFESP)
Abstract The selective distribution of methionyl aminopeptidase (MAP) among rat liver mitochondria (heavy and light) and microsomes is reported. Several properties of MAP from the three subcellular fractions showed that the enzyme is a typical aminopeptidase able to remove N-terminal methionine from oligopeptides and methionyl-2-naphthylamide but not from Met-Ala-Ser. MAP is a membrane-bound enzyme sensitive to SH-group oxidants and inhibitable by L-methionine but not by usual arylaminopeptidase inhibitors. It is suggested that, MAP may play an important role during protein synthesis in rat liver.
Keywords METHIONYL AMINOPEPTIDASE
N-TERMINAL METHIONINE
AMINOPEPTIDASE
ARYLAMIDASE
RAT LIVER
Language English
Date 1991-04-10
Published in Molecular And Cellular Biochemistry. Dordrecht: Kluwer Academic Publ, v. 102, n. 2, p. 101-113, 1991.
ISSN 0300-8177 (Sherpa/Romeo, impact factor)
Publisher Kluwer Academic Publ
Extent 101-113
Origin http://dx.doi.org/10.1007/BF00234568
Access rights Open access Open Access
Type Article
Web of Science ID WOS:A1991FG12900002
URI http://repositorio.unifesp.br/11600/44921

Show full item record




File

File Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Search


Browse

Statistics

My Account