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Class II tubulin, the major brain β tubulin isotype is polyglutamylated on glutamic acid residue 435
Author(s) -
Rüdiger Manfred,
Plessman Uwe,
Klöppel Klaus-Dieter,
Wehland Jürgen,
Weber Klaus
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81061-p
Subject(s) - edman degradation , tubulin , isotype , glutamic acid , residue (chemistry) , biochemistry , biology , subtilisin , peptide sequence , microbiology and biotechnology , amino acid , chemistry , microtubule , antibody , immunology , enzyme , monoclonal antibody , gene
Protein sequencing shows that porcine brain tubulin retains the N‐terminal sequences of α and β tubulin after a mild treatment with subtilisin, C‐terminal peptides released by subtilisin were purified and characterized by automated Edman degradation and mass spectrometry. We confirm the polyglutamylation of α tubulin on glutamic acid residue 445 reported by others and show in addition that class 11 β tubulin, the major β tubulin isotype of adult brain, is also polyglutamylated. The substitution is restricted to glutamic acid residue 435. Thus all major tubulin isotypes of adult brain are subjected to polyglutamylation.