| Literature DB >> 728448 |
Abstract
The alpha-chain of calf brain tubulin was fragmented by treatment with cyanogen bromide and eight peptides together accounting for 108 residues were purified and sequenced. The COOH-terminal peptide contains a fractional amount (about 0.3 residues) of tyrosine at its COOH-terminus; this presumably represents tyrosine that is added post-translationally to alpha-tubulin. The beta-chain can be phosphorylated, and the probable site of this modification is identified also in the COOH-terminal peptide. Comparison of the sequences described here with the sequence of actin reveals no homology between actin and tubulin.Entities:
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Year: 1978 PMID: 728448 DOI: 10.1016/0005-2795(78)90515-9
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002