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Volumn 414, Issue 1, 1997, Pages 39-44
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C-terminal truncation of thymosin β10 by an intracellular protease and its influence on the interaction with G-actin studied by ultrafiltration
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Author keywords
thymosin; Actin; Dissociation constant; Proteolytic modification; Rabbit spleen; Ultrafiltration
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Indexed keywords
G ACTIN;
THYMOSIN;
AMINO ACID ANALYSIS;
ANIMAL TISSUE;
ARTICLE;
CONTROLLED STUDY;
MASS SPECTROMETRY;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN ANALYSIS;
PROTEIN DEGRADATION;
PROTEIN EXPRESSION;
PROTEIN ISOLATION;
PROTEIN PROTEIN INTERACTION;
RABBIT;
SPLEEN;
STRUCTURE ACTIVITY RELATION;
TEMPERATURE;
ACTINS;
AMINO ACIDS;
ANIMALS;
CELL LINE;
CHROMATOGRAPHY, HIGH PRESSURE LIQUID;
ENDOPEPTIDASES;
HUMANS;
LUNG;
PEPTIDE FRAGMENTS;
RABBITS;
SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;
SPLEEN;
TEMPERATURE;
THYMOSIN;
ULTRAFILTRATION;
ANIMALIA;
MAMMALIA;
ORYCTOLAGUS CUNICULUS;
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EID: 0343852690
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(97)00946-0 Document Type: Article |
Times cited : (22)
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References (34)
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