Dependence of the length of the heavy chain of chymotryptic subfragment 1 on the temperature of myosin digestion

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 obtai...

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Bibliographic Details
Published in:FEBS letters 1989-01, Vol.243 (1), p.30-32
Main Authors: Pliszka, Barbara, Rȩdowicz, Maria J., Strzelecka-Gołaszewska, Hanna
Format: Article
Language:English
Subjects:
1,5-IAEDANS, N-iodoacetyl-N′-(5-sulfo-1-naphthyl)ethylenediamine
Animals
chymotrypsin
Chymotrypsin - metabolism
Chymotryptic cleavage
HMM, heavy meromyosin
Kinetics
Macromolecular Substances
Molecular Weight
Muscles - enzymology
Myosin
Myosins - metabolism
Peptide Fragments - metabolism
Rabbits
S1, myosin subfragment 1
SDS-PAGE, SDS-polyacrylamide gel electrophoresis
skeletal muscle
Subfragment 1
temperature
Temperature dependence
Thermodynamics
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)81211-6