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Volumn 72, Issue , 2015, Pages 6-10
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Expression, purification and thermostability of MBP-chondroitinase ABC I from Proteus vulgaris
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Author keywords
Characterization; Expression; MBP chondrotinase ABC I; Productivity; Thermostability
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Indexed keywords
CHONDROITIN ABC I;
CHONDROITIN ABC LYASE;
MALTOSE BINDING PROTEIN;
UNCLASSIFIED DRUG;
CHONDROITIN 4 SULFATE;
CHONDROITINASE ABC I;
HYBRID PROTEIN;
ARTICLE;
CONTROLLED STUDY;
DNA SEQUENCE;
ENZYME ACTIVITY;
ENZYME DEGRADATION;
ENZYME PURIFICATION;
ESCHERICHIA COLI;
FERMENTATION;
NONHUMAN;
PH;
PROCESS OPTIMIZATION;
PROTEIN EXPRESSION;
PROTEIN PROTEIN INTERACTION;
PROTEIN PURIFICATION;
PROTEIN SYNTHESIS;
PROTEUS VULGARIS;
TEMPERATURE SENSITIVITY;
THERMOSTABILITY;
CHSASE ABC I GENE;
ENZYME ANALYSIS;
ENZYME SPECIFICITY;
ENZYME STABILITY;
ENZYME SUBSTRATE;
MOLECULAR CLONING;
NUCLEOTIDE SEQUENCE;
PLASMID;
TEMPERATURE;
BACTERIAL GENE;
BIOCATALYSIS;
ENZYMOLOGY;
GENETICS;
ISOLATION AND PURIFICATION;
KINETICS;
METABOLISM;
PROTEUS VULGARIS;
BIOCATALYSIS;
CHONDROITIN ABC LYASE;
ENZYME STABILITY;
GENES, BACTERIAL;
HYDROGEN-ION CONCENTRATION;
KINETICS;
MALTOSE-BINDING PROTEINS;
PLASMIDS;
PROTEUS VULGARIS;
RECOMBINANT FUSION PROTEINS;
SEQUENCE ANALYSIS, DNA;
TEMPERATURE;
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EID: 84906336174
PISSN: 01418130
EISSN: 18790003
Source Type: Journal
DOI: 10.1016/j.ijbiomac.2014.07.040 Document Type: Article |
Times cited : (22)
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References (23)
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