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Research Database PMU-SQQUID

Isolation and sequence of a tropomyosin-binding fragment of turkey gizzard calponin.
Vancompernolle, K; Gimona, M; Herzog, M; Van Damme, J; Vandekerckhove, J; Small, V;
FEBS Lett. 1990; 274(1-2): 146-150.
Originalarbeiten (Zeitschrift)

PMU-Authors

Gimona Mario

Abstract

Limited chymotryptic cleavage of turkey gizzard calponin yields a 13 kDa fragment which could be purified by its ability to bind to Sepharose-immobilized tropomyosin. This 13 kD polypeptide is shown to be derived from a 22 kDa fragment. Complete amino acid sequence analysis of the 13 kD and 22 kD fragments reveals high homology with the formerly characterized smooth muscle-specific protein SM22 alpha (Pearlstone, J.R., Weber, M., Lees-Miller, J.P., Carpenter, M.R. and Smillie L.B., 1987, J. Biol. Chem. 262, 5985-5991) and the product of gene mp20 of Drosophila (Ayme-Southqate, A., Lasko, P., French, C, and Pardue, M.L. [(1989) J. Cell Biol. 108, 521-531]. Futhermore we recognize sequence elements of a putative actin-binding domain of alpha-actinin, the calpactin I or p 36 sequence, and a consensus motif present in the repeats of the gene product of the candidate unc-87 gene of C. elegans (S.D. Goetinck and R.H. Waterston, personal communication).


Useful keywords (using NLM MeSH Indexing)

Amino Acid Sequence

Animals

Binding Sites

Calcium-Binding Proteins/genetics

Calcium-Binding Proteins/isolation*

purification

Calcium-Binding Proteins/metabolism*

Chymotrypsin

Cyanogen Bromide

Gizzard/metabolism

Microfilament Proteins

Molecular Sequence Data

Muscle Proteins/metabolism*

Muscle, Smooth/metabolism*

Peptide Fragments/isolation*

purification

Peptide Fragments/metabolism

Sequence Homology, Nucleic Acid

Tropomyosin/metabolism

Turkeys