000088445 001__ 88445
000088445 005__ 20181203020500.0
000088445 0247_ $$2doi$$a10.1111/j.1432-1033.1989.tb14610.x
000088445 037__ $$aARTICLE
000088445 245__ $$aPurification and characterization of a methionine-specific aminopeptidase from Salmonella typhimurium
000088445 269__ $$a1989
000088445 260__ $$c1989
000088445 336__ $$aJournal Articles
000088445 520__ $$aAn aminopeptidase specific for methionine (peptidase M) has been purified from wild-type and mutant Salmonella typhimurium strains. Recombinant peptidase M was also purified from Escherichia coli. These preparations were characterized with respect to their physicochemical properties using analytical ultracentrifugation, SDS/PAGE, isoelectric focusing, titration curve analysis, amino acid analysis, N- and C-terminal sequencing and various spectroscopic methods. Peptidase M activity is stimulated by Co2+, in agreement with previous studies using crude extracts of Salmonella. The purified preparations did not contain significant amounts of any metal. Enzymically important metal is loosely associated and lost during enzyme purification. Peptidase M was shown to contain seven free sulphydryl residues none of which are involved in either intra- or inter-molecular disulphide bonds. Most appear solvent-accessible as evidenced by their reactivity under native conditions. Limited modification of the sulphydryl residues with either iodoacetamide of 5,5'-dithiobis(2-nitrobenzoic acid) led to inactivation. Several cysteines were shown to be labelled to various degrees by peptide mapping of inactivated S-[14C]carboxymethylated protein. Whether cysteine modification affects enzymic activity directly (blocking an active site) or indirectly (by causing conformational change) remains to be established.
000088445 6531_ $$aaminopeptidase
000088445 6531_ $$amethionine
000088445 6531_ $$amicrosomal aminopeptidase
000088445 6531_ $$asalmonella typhimurium
000088445 700__ $$aWingfield, P.
000088445 700__ $$aGraber, P.
000088445 700__ $$0240363$$aTurcatti, G.$$g103994
000088445 700__ $$aMovva, N. R.
000088445 700__ $$aPelletier, M.
000088445 700__ $$aCraig, S.
000088445 700__ $$aRose, K.
000088445 700__ $$aMiller, C. G.
000088445 773__ $$j180$$k1$$q23-32$$tEuropean Journal of Biochemistry
000088445 909C0 $$0252118$$pPTCB$$xU11378
000088445 909CO $$ooai:infoscience.tind.io:88445$$pSV$$particle
000088445 937__ $$aEPFL-ARTICLE-88445
000088445 970__ $$a23/BSF
000088445 973__ $$aOTHER$$sPUBLISHED
000088445 980__ $$aARTICLE