Open AccessComplete amino acid sequence of alpha-tubulin from porcine brain.
Author(s) -
Herwig Ponstingl,
Erika Krauhs,
Melvyn Little,
Tore Kempf
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.5.2757
Subject(s) - edman degradation , tubulin , tyrosine , amino acid , tropomyosin , peptide sequence , biochemistry , melittin , alpha (finance) , protein primary structure , biology , sequence (biology) , actin , chemistry , microtubule , stereochemistry , microbiology and biotechnology , peptide , genetics , gene , medicine , construct validity , nursing , patient satisfaction
The amino acid sequence of alpha-tubulin from porcine brain was determined by automated and manual Edman degradation of eight sets of overlapping peptides. It comprises 450 residues plus a COOH-terminal tyrosine that is present only in 15% of the material. A region of 40 residues at the COOH-terminus is highly acidic, mainly due to 16 glutamyl residues. This high concentration of negative charge suggests a region for binding cations. At least six positions, most of them around position 270, are occupied by two amino acid residues each. Several of these exchange sites were assigned to specific peptides by analysis of the purified corresponding fragments. These data indicate four alpha-tubulins in porcine brain. Although alpha-tubulin on the whole is unrelated to other proteins, there are regions that can be correlated to sequences of the myosin head, to actin, to tropomyosin, and to troponins C and T.