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Selective cleavage of the connector segments within the myosin‐S1 heavy chain by staphylococcal protease
Author(s) -
Chaussepied P.,
Bertrand R.,
Audemard E.,
Pantel P.,
Derancourt J.,
Kassab R.
Publication year - 1983
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(83)80735-2
Subject(s) - myosin , protease , cleavage (geology) , actin , chemistry , biochemistry , peptide sequence , trypsin , amino acid , microbiology and biotechnology , enzyme , biology , gene , paleontology , fracture (geology)
The existence of the two connector segments linking the tryptic 50 kDA fragment of skeletal S1 heavy chain to the adjacent 27 kDa and 20 kDa peptides was ascertained by digestion of S1 with staphylococcal protease which was found to act specifically at these particular regions. Three new peptides of M r 28 000, 48 000 and 22 000 were produced and the novel S1 derivative formed had an intact actin‐activated ATPase activity. Amino acid sequence analyses indicated that the 48 kDa and 22 kDa peptides overlap the two connector elements.