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Journal ArticleDOI

A chemical comparison of tropomyosins from muscle and non-muscle tissues.

Richard E. Fine, +1 more
- 05 Jul 1975 - 
- Vol. 95, Iss: 3, pp 447-454
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TLDR
Findings indicate that muscle and non-muscle tropomyosins are grouped into two similar but non-identical classes of protein, and is likely that both gene classes evolved from an ancestral gene by a process involving gene duplication.
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This article is published in Journal of Molecular Biology.The article was published on 1975-07-05. It has received 145 citations till now. The article focuses on the topics: Tropomyosin & Skeletal muscle.

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Citations
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Journal ArticleDOI

Identification and characterization of multiple forms of actin

TL;DR: Multiple forms of actin have been found in a variety of mammalian cell lines and tissues by the use of high resolution, two-dimensional gel electrophoresis, andryptic peptide comparisons have shown that muscle actin is distinguished from the two "nonmuscle" actins by several peptide differences, and that the two non-muscle actins are nearly identical.
Journal ArticleDOI

Vertebrate tropomyosin: distribution, properties and function.

TL;DR: In the case of muscle there is clear evidence that the TM moves its position on the F-actin filament during contraction and it is therefore considered to play an important part in the regulation of the process.
Journal Article

HHF35, a muscle-actin-specific monoclonal antibody. I. Immunocytochemical and biochemical characterization.

TL;DR: Immunocytochemical analysis of methanol-Carnoy's-fixed, paraffin-embedded human tissue revealed that this monoclonal antibody, termed HHF35, reacts with skeletal Muscle cell actin isotypes, but is nonreactive with endothelial, epithelial, neural, or connective tissue cells.
Journal ArticleDOI

The 14-fold periodicity in α-tropomyosin and the interaction with actin

TL;DR: It is proposed that the seven α and seven β bands are alternative sets of sites which bind equivalently to complementary groups of sites on seven actins in the “relaxed” and “active” states of muscle, respectively.
References
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Journal ArticleDOI

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis

TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
Journal ArticleDOI

Fluorometric assay of proteins in the nanogram range

TL;DR: The reagent fluorescamine has been used for the fluorometric assay of proteins based on their content of free amino groups and its applications to the monitoring of proteins during enzyme purification are described.
Journal ArticleDOI

Strategy and tactics in protein chemistry.

B S Hartley
- 01 Oct 1970 - 
Journal ArticleDOI

Amino-terminal Sequence Analysis of Proteins Purified on a Nanomole Scale by Gel Electrophoresis

TL;DR: In this modification of the 5-dimethylaminonaphthalene-1-sulfonyl-Edman degradation, inorganic carriers permit convenient manipulation of small amounts of protein, and use of the detergent sodium dodecyl sulfate throughout the procedure maintains protein solubility.
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