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Volumn 329, Issue 2, 2004, Pages 345-347
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Escherichia coli methionine aminopeptidase with Tyr168 to alanine substitution can improve the N-terminal processing of recombinant proteins with valine at the penultimate position
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Author keywords
[No Author keywords available]
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Indexed keywords
ESCHERICHIA COLI;
RECOMBINANT PROTEINS;
ALANINE SUBSTITUTION;
METHIONINE AMINOPEPTIDASE;
N-TERMINALS;
AMINO ACIDS;
ALANINE;
METHIONYL AMINOPEPTIDASE;
RECOMBINANT PROTEIN;
TYROSINE DERIVATIVE;
VALINE;
AMINO ACID SUBSTITUTION;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CONTROLLED STUDY;
ENZYME ACTIVITY;
ESCHERICHIA COLI;
HIGH PERFORMANCE LIQUID CHROMATOGRAPHY;
MOLECULAR DYNAMICS;
MOLECULAR INTERACTION;
MOLECULAR MECHANICS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
PROTEIN ISOLATION;
PROTEIN PURIFICATION;
REACTION ANALYSIS;
REACTION OPTIMIZATION;
STRUCTURE ANALYSIS;
SUBSTITUTION REACTION;
WILD TYPE;
ESCHERICHIA COLI;
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EID: 2542417350
PISSN: 00032697
EISSN: None
Source Type: Journal
DOI: 10.1016/j.ab.2004.03.031 Document Type: Article |
Times cited : (2)
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References (6)
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