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Thermal stability of myosin subfragment‐1 decreases upon tryptic digestion in the presence of nucleotides
Author(s) -
Pintér Katalin,
Lu Renne Chen,
Szilágyi László
Publication year - 1986
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(86)80542-7
Subject(s) - myosin , chemistry , nucleotide , digestion (alchemy) , thermal stability , biochemistry , chromatography , organic chemistry , gene
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 aminoterminal fragment between Arg 23 and Ile 24.