caa a22 4500 397556055 CHVBK 20180308164802.0 cr unu---uuuuu 161202e199606 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021344 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021344 Structure of Heads A and B of Myosin Studied by Tryptic Digestion of Myosin Subfragment-1 [Elektronische Daten] [Shin Murai, Toshiaki Arata, Akio Inoue] We studied the difference in the structure of head B (P1 -burst head) and head A of myosin by limited tryptic digestion of myosin subfragment-1 (S-l), and using antibodies (anti-A and anti-B) which bind specifically with each head. The antibodies were prepared using peptides with sequences identical to those around the reactive lysine residue of heads A and B. When myosin subfragment-1 (S-l) was cleaved limitedly by trypsin, S-1 heavy chain (100 kDa) was digested into fragments of 25,50, and 20 kDa. Two fragments with molecular masses of 75 and 27 kDa were transiently produced in the initial phase of digestion. Anti-A and anti-B antibodies bound only with peptides that contained the reactive lysine residue [S-1 heavy chain (100 kDa), 75-, 27-, and 25-kDa peptides], thus showing specific binding with antigen peptide. However, the 27-kDa fragment bound more strongly with anti-B antibody than with anti-A antibody. When S-l was separated into fractions rich in S-1A and S-1B using insoluble anti-A or anti-B antibody, each antibody bound more strongly with the S-l heavy chain (100 kDa) of its corresponding fraction by Western immunoblotting. These results suggest that the antibodies react specifically with peptides even after SDS-PAGE and membrane-blotting, and that the structure of the 25 kDa-50 kDa junction differs between heads A and B of myosin. © by the Journal of Biochemistry Regular Papers nationallicence muscle nationallicence myosin nationallicence myosin heads nationallicence subfragment-1 nationallicence Murai Shin Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560 aut Arata Toshiaki Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560 aut Inoue Akio Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560 aut The Journal of Biochemistry Oxford University Press 119/6(1996-06), 1033-1037 0021-924X 119:6<1033 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021344 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021344 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Murai Shin Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560 aut NATIONALLICENCE 700 1- Arata Toshiaki Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560 aut NATIONALLICENCE 700 1- Inoue Akio Department of Biology, Faculty of Science, Osaka University, Toyonaka, Osaka 560 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/6(1996-06), 1033-1037 0021-924X 119:6<1033 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford