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PMID: 7019911 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Complete amino acid sequence of alpha-tubulin from porcine brain.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 78 ·No. 5 ·1981-05-00 ·Pages 2757-61

Ponstingl H, Krauhs E, Little M, Kempf T

Abstract

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.

MeSH Terms
Animals Brain Chemistry Cyanogen Bromide Macromolecular Substances Peptide Fragments/analysis Peptide Hydrolases Protein Conformation Swine Tubulin/isolation & purification
Chemicals
Macromolecular Substances Peptide Fragments Tubulin Peptide Hydrolases Cyanogen Bromide
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ponstingl H
Krauhs E
Little M
Kempf T
References (33)
33 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.78.5.2757
Published
1981-05-00
Pages
2757-61
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC319436
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.78.5.2757 PMC Full Text View journal details
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