Synthetic peptides identify the minimal substrate requirements of tubulin polyglutamylase in side chain elongation

FEBS Letters

Volumn 459, Issue 1, 1999, Pages 90-94

  Westermann, Stefan ^a   Plessmann, Uwe ^a   Weber, Klaus ^a  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Crithidia fasciculata; Polyglutamylation; Post translational modification; Trypanosomatid; Tubulin

Indexed keywords

CHOLESTEROL MONOOXYGENASE (SIDE CHAIN CLEAVING); POLYGLUTAMIC ACID; SYNTHETIC PEPTIDE; TUBULIN;

ANION EXCHANGE CHROMATOGRAPHY; ARTICLE; CONTROLLED STUDY; CRITHIDIA FASCICULATA; CYTOSKELETON; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SUBSTRATE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PROCESSING; TRYPANOSOMA;

AMINO ACID SEQUENCE; ANIMALS; BRAIN; CRITHIDIA FASCICULATA; IMMUNOBLOTTING; MOLECULAR SEQUENCE DATA; PEPTIDE SYNTHASES; PEPTIDES; POLYGLUTAMIC ACID; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TUBULIN;

CRITHIDIA; CRITHIDIA FASCICULATA; TRYPANOSOMATIDAE;

EID: 0032835183     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)01227-2     Document Type: Article

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