Results 81 to 90 of about 2,569 (110)

Purification and properties of N-formylmethionine aminopeptidase from rat liver

Biochimica Et Biophysica Acta - Biomembranes, 1980
A specific enzyme for the liberation of N-terminal N-formylmethionine from N-formylmethionyl peptides was purified 4750-fold from rat liver by successive applications of (NH4)SO4 precipitation, DEAE-cellulose, N-formylbestatin-AH-Sepharose 4B and AH-Sepharose 4B chromatography followed by Sepharose CL-6B gel filtration.
Hiroyuki Suda
exaly   +3 more sources

Isolation and purification of N-formylmethionine aminopeptidase from rat intestine

BBA - Proteins and Proteomics, 1992
The intestinal mucosal epithelium is exposed to products of intestinal bacteria including potent inflammatory N-formylmethionyl oligopeptides. An N-formylmethionine aminopeptidase has been purified 2300-fold from rat intestine and was shown to degrade natural fMet oligopeptides from Escherichia coli culture supernatants with loss of bioactivity ...
V S Chadwick
exaly   +3 more sources

N-formylmethionine: the N terminus of Clostridium pasteurianum rubredoxin

Biochemical and Biophysical Research Communications, 1970
Abstract The N terminal amino acid of C. pasteurianum rubredoxin has been determined to be N-formylmethionine.
Walter Lovenberg
exaly   +3 more sources

Ab initio- and density-functional studies of conformational behaviour of N-formylmethionine in gaseous phase

Chemical Papers, 2014
AbstractThe current work is a study of the conformational space of the non-ionic N-formylmethionine molecule around its seven structurally significant internal backbone torsional angles at B3LYP/6-31++G(d,p) levels of theory in the gaseous phase. The potential energy surface exploration reveals that a total of 432 different conformers would result if ...
Gunajyoti Das, Shilpi Mandal
exaly   +2 more sources

Increased peptide deformylase activity for N-formylmethionine processing of proteins overexpressed in Escherichia coli: application to homogeneous rubredoxin production

Protein Expression and Purification, 2004
Deformylation of the initiator N-formylmethionine does not always proceed to completion for proteins overexpressed in Escherichia coli. To overcome this limitation, the def gene encoding the Escherichia coli peptide deformylase was cloned into the plysS plasmid under the tetracycline (Tc) promoter control.
David Lemaster
exaly   +6 more sources

Methylprednisolone reduces airway microvascular permeability but not airway resistance induced by N-formylmethionine leucyl-phenylalanine in the rabbit

Respirology, 2004
Objective:  The aim of this study was to determine the effect of corticosteroids on the increase in airway microvascular permeability (MVP) and airway resistance induced by N‐formylmethionine leucyl‐phenylalanine in the rabbit.Methodology:  After pretreatment with methylprednisolone (for 1 day or 1 week) rabbits were nebulized with N‐formylmethionine ...
Melissa, Matheson, Melissa, McClean, Ann-Christine, Rynell, Norbert, Berend   +3 more
exaly   +3 more sources

A pan-N-formylmethionine-specific antibody as a tool for analyzing Nα-terminal formylation

Methods in Enzymology
Formylmethionine (fMet) plays crucial roles across bacterial and eukaryotic systems, contributing to protein translation, degradation, complex formation, stress adaptation, disease progression, and immune response. However, detecting fMet-bearing (fMet-) peptides and proteins has remained challenging due to the lack of effective anti-pan-fMet ...
Eun-Jin Lee, Cheol-Sang Hwang, Chang-Seok Lee   +2 more
exaly   +3 more sources

Deformylation of N-formylmethionine by Escherichiacoli extracts

Biochemical and Biophysical Research Communications, 1967
Herbert Weissbach, Betty Redfield, B Redfield   +2 more
exaly   +3 more sources