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Cited by 305

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

Open access
Krauhs, E, Little, M, Kempf, T, Hofer-Warbinek, R, Ade, W, Ponstingl, H·1981·Proceedings of the National Academy of Sciences

Abstract

The primary structure of porcine brain beta-tubulin was determined by automated and manual Edman degradation of six sets of overlapping peptides. The protein consists of 445 amino acid residues and has a minimum of six positions that are heterogeneous, indicating at least two beta-tubulins in porcine brain. Comparison of the optimally aligned sequences of alpha-tubulin and beta-tubulin indicates that 41% of their primary structures are identical. A region rich in glycyl residues is similar both in sequence and predicted secondary structure to the phosphate binding loop of several nucleotide binding enzymes. beta-Tubulin contains a highly acidic COOH-terminal region that resembles the NH2-terminus of troponin T.

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Metadata

Authors
Krauhs, E., Little, M., Kempf, T., Hofer-Warbinek, R., Ade, W., & Ponstingl, H.
Venue
Proceedings of the National Academy of Sciences
Published
1981-07
Volume
78
Issue
7
Pages
4156-4160
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1990343615
Cited by
305
References
0
FWCI
11.37
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Complete amino acid sequence of beta-tubulin from porcine brain. https://app.cochat.ai/papers/10.1073/pnas.78.7.4156
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Krauhs, E., Little, M., Kempf, T., Hofer-Warbinek, R., Ade, W., & Ponstingl, H. (1981). Complete amino acid sequence of beta-tubulin from porcine brain. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.78.7.4156

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