Thermal stability of myosin subfragment-1 decreases upon tryptic digestion in the presence of nucleotides

FEBS Lett. 1986 May 5;200(1):221-5. doi: 10.1016/0014-5793(86)80542-7.

Abstract

Myosin subfragment-1 (S-1), digested with trypsin in the presence of ATP, rapidly loses its ATPase activity upon mild heat treatment even if ATP or ADP is present. The heat-treated molecule is very sensitive to further tryptic digestion. Undigested S-1 and S-1 digested in the absence of ATP are protected by nucleotides. The loss of the protective effect of nucleotides correlates with the tryptic splitting of the 25 kDa amino-terminal fragment between Arg 23 and Ile 24.

MeSH terms

  • Adenosine Diphosphate / pharmacology*
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / pharmacology*
  • Chymotrypsin / metabolism
  • Drug Stability
  • Hot Temperature
  • Kinetics
  • Molecular Weight
  • Myosin Subfragments
  • Myosins / metabolism*
  • Peptide Fragments / metabolism*
  • Trypsin / metabolism

Substances

  • Myosin Subfragments
  • Peptide Fragments
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Chymotrypsin
  • Trypsin
  • Adenosine Triphosphatases
  • Myosins