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Amino acid sequence of chicken gizzard gamma-tropomyosin.
Chicken gizzard muscle tropomyosin has been fractionated into its two major components, beta and gamma and the amino acid sequence of the gamma component established by the isolation and sequence analysis of fragments derived from cyanogen bromide cleavage and tryptic digestions. Despite its much slower mobility on sodium dodecyl sulfate-polyacrylamide electrophoretic gels, it has the same polypeptide chain length (284 residues) as the alpha and beta components of rabbit skeletal muscle. Evidence for microheterogeneity of the chicken gizzard component was detected both on electrophoretic gels and in the sequence analysis. The gamma component is more closely related to rabbit skeletal alpha-tropomyosin than to the beta component. While the protein is highly homologous to the rabbit skeletal tropomyosins, significant sequence differences are observed in two regions; between residues 42-83 and 258-284. In the latter region (COOH-terminal) the alterations in sequence are very similar to those seen in platelet tropomyosin when compared with the skeletal proteins.
PMID: 3997866 [PubMed - indexed for MEDLINE]
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Cited by 7 PubMed Central articles
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Predicting coiled coils by use of pairwise residue correlations.
Berger B, Wilson DB, Wolf E, Tonchev T, Milla M, Kim PS.
Proc Natl Acad Sci U S A. 1995 Aug 29; 92(18):8259-63.
[Proc Natl Acad Sci U S A. 1995]
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Isolation, sequence, and developmental profile of a brain-specific polypeptide, PEP-19.
Ziai R, Pan YC, Hulmes JD, Sangameswaran L, Morgan JI.
Proc Natl Acad Sci U S A. 1986 Nov; 83(21):8420-3.
[Proc Natl Acad Sci U S A. 1986]
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The rat alpha-tropomyosin gene generates a minimum of six different mRNAs coding for striated, smooth, and nonmuscle isoforms by alternative splicing.
Wieczorek DF, Smith CW, Nadal-Ginard B.
Mol Cell Biol. 1988 Feb; 8(2):679-94.
[Mol Cell Biol. 1988]
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