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Volumn 151, Issue 2-3, 2008, Pages 512-521
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Purification and biochemical characterization of methionine aminopeptidase (MetAP) from mycobacterium smegmatis mc2155
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Author keywords
l methionine p nitroanilide; Metalloenzyme; Methionine aminopeptidases; Mycobacterium smegmatis mc2 155; Peptide processing
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Indexed keywords
L-METHIONINE P-NITROANILIDE;
METALLOENZYME;
METHIONINE AMINOPEPTIDASES;
MYCOBACTERIUM SMEGMATIS MC2 155;
PEPTIDE PROCESSING;
AMINES;
DIFFUSERS (OPTICAL);
ELECTROPHORESIS;
ENZYMES;
GELATION;
GELS;
METAL RECOVERY;
METAL REFINING;
POLYMERS;
PURIFICATION;
SODIUM;
SODIUM SULFATE;
ENZYME ACTIVITY;
4 NITROANILINE;
COBALT;
COPPER;
EDETIC ACID;
MAGNESIUM;
METHIONINE;
METHIONYL AMINOPEPTIDASE;
ACTINONIN;
AMASTATIN;
AMINOPEPTIDASE;
BESTATIN;
CALCIUM CHLORIDE;
COBALT CHLORIDE;
CUPRIC CHLORIDE;
DRUG DERIVATIVE;
FERROUS CHLORIDE;
FERROUS ION;
HYDROXAMIC ACID;
LEUCINE;
MAGNESIUM CHLORIDE;
PEPTIDE;
ARTICLE;
ENZYME ANALYSIS;
ENZYME PURIFICATION;
IN VITRO STUDY;
MYCOBACTERIUM SMEGMATIS;
NONHUMAN;
PH;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
TEMPERATURE;
CHEMISTRY;
DRUG ANTAGONISM;
ENZYME STABILITY;
ENZYMOLOGY;
ISOLATION AND PURIFICATION;
METABOLISM;
MOLECULAR WEIGHT;
MYCOBACTERIUM SMEGMATIS;
AMINOPEPTIDASES;
CALCIUM CHLORIDE;
COBALT;
COPPER;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ENZYME STABILITY;
FERROUS COMPOUNDS;
HYDROGEN-ION CONCENTRATION;
HYDROXAMIC ACIDS;
LEUCINE;
MAGNESIUM CHLORIDE;
MOLECULAR WEIGHT;
MYCOBACTERIUM SMEGMATIS;
PEPTIDES;
TEMPERATURE;
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EID: 58149187355
PISSN: 02732289
EISSN: None
Source Type: Journal
DOI: 10.1007/s12010-008-8227-y Document Type: Article |
Times cited : (10)
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References (33)
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