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Digestion of tropomyosin with trypsin
Author(s) -
Gorecka A.,
Drabikowski W.
Publication year - 1977
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(77)80072-0
Subject(s) - tropomyosin , citation , library science , trypsin , chemistry , biochemistry , computer science , myosin , enzyme
Tropomyosin is a rod-like a-helical protein composed of two similar subunits in a coiled-coil configuration. It is situated in the grooves of the F-actin strands and with troponin constitutes the regulatory-complex of vertebrate striated muscle. The sequence of the tropomyosin subunit has been determined by Stone, et al. [ 11. As a result of this work it was recognized that a repeat sequence existed [l-3] which correlated to the 7 actin binding sites along the tropomyosin molecule [4]. The location of the troponin binding site has also been established [5]. Since the biological and physical properties of tropomyosin are so well defined and related to its primary structure it seemed to be an ideal protein to study with respect to its fragmentation by trypsin. The object being to examine variqus tryptic fragments and determine whether these retain any of the properties of the native molecule.