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Dependence of the length of the heavy chain of chymotryptic subfragment 1 on the temperature of myosin digestion
Author(s) -
Pliszka Barbara,
Rȩdowicz Maria J.,
Strzelecka-Gołaszewska Hanna
Publication year - 1989
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(89)81211-6
Subject(s) - myosin , chemistry , chymotrypsin , digestion (alchemy) , heavy chain , divalent , chain (unit) , biochemistry , crystallography , enzyme , trypsin , chromatography , organic chemistry , physics , astronomy , gene
Limited digestion of filamentous myosin with chymotrypsin at 0°C in the absence of divalent cations generates two forms of subfragment 1 (S1), with heavy chains of 95 kDa and 98 kDa. The difference is at the C‐terminal end of the chain. The 98 kDa form prevails, in contrast to the preparations obtained by digestion at room temperature which consist of the shorter species and only traces of the longer one. The results support the idea of a temperature‐dependent conformational transition at the head‐rod junctional region of the myosin heavy chain.