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Volumn 25, Issue 8, 2012, Pages 405-413
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A low-cost affinity purification system using β-1,3-glucan recognition protein and curdlan beads
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Author keywords
1,3 glucan recognition protein; affinity tag; curdlan; glutathione S transferase; recombinant protein
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Indexed keywords
AFFINITY PURIFICATION;
AFFINITY TAG;
ALKALINE SOLUTIONS;
CREATIVE COMMONS;
CURDLAN;
EXPRESSION LEVELS;
GLUTATHIONE-S-TRANSFERASE;
GLUTATHIONES;
LOW COSTS;
OPEN ACCESS;
OXFORD UNIVERSITY;
SOLUBLE FRACTION;
TAGGED PROTEINS;
ALKALINITY;
CENTRIFUGATION;
PURIFICATION;
RECOMBINANT PROTEINS;
STRUCTURAL ANALYSIS;
FOOD ADDITIVES;
BETA 1,3 GLUCAN;
BETA 1,3 GLUCAN RECOGNITION PROTEIN;
BINDING PROTEIN;
CURDLAN;
CURDLAN BEAD;
GLUTATHIONE;
GLUTATHIONE TRANSFERASE;
RECOMBINANT PROTEIN;
UNCLASSIFIED DRUG;
ARTICLE;
BINDING AFFINITY;
CENTRIFUGATION;
COMPLEX FORMATION;
MOLECULAR INTERACTION;
MOLECULAR RECOGNITION;
NONHUMAN;
NUCLEOTIDE SEQUENCE;
PH;
PRIORITY JOURNAL;
PROTEIN DETERMINATION;
PROTEIN DOMAIN;
PROTEIN EXPRESSION;
PROTEIN FUNCTION;
PROTEIN PURIFICATION;
PROTEIN STABILITY;
PROTEIN STRUCTURE;
SILKWORM;
SOLUBILIZATION;
ULTRASOUND;
AMINO ACID SEQUENCE;
ANIMALS;
BASE SEQUENCE;
BETA-GLUCANS;
BOMBYX;
CARRIER PROTEINS;
CHROMATOGRAPHY, AFFINITY;
DEAD-BOX RNA HELICASES;
ESCHERICHIA COLI;
GLUTATHIONE TRANSFERASE;
HUMANS;
INSECT PROTEINS;
MOLECULAR SEQUENCE DATA;
PROTEIN STABILITY;
RECOMBINANT FUSION PROTEINS;
BOMBYX MORI;
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EID: 84863702142
PISSN: 17410126
EISSN: 17410134
Source Type: Journal
DOI: 10.1093/protein/gzs028 Document Type: Article |
Times cited : (9)
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References (20)
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