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Structural differences between myofibrillar protein, paratropomyosin, and tropomyosin as revealed by high‐performance liquid chromatography
Author(s) -
Nishio Yuriko,
Ushimura Yuichi,
Ueda Shuji,
Maeda Naoyuki,
Hattori Akihito,
Yamanoue Minoru
Publication year - 2018
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/asj.13022
Subject(s) - tropomyosin , myofibril , high performance liquid chromatography , chemistry , myosin , gene isoform , protein subunit , amino acid , chromatography , biochemistry , disulfide bond , gene
Paratropomyosin ( PTM ) composes myofibril functions to weaken the rigor linkages formed between actin and myosin during postmortem aging of muscles. PTM has the similar physico‐chemical properties as tropomyosin ( TM ) that is a regulatory protein of myofibrils. So far, it is unclear whether PTM is definitely different from TM , because the primary structure of PTM has not been determined yet. The aim of this study was to clarify structural difference of PTM from TM . PTM was prepared by column chromatography immediately after slaughter from broiler breast muscle, and purified by high‐performance liquid chromatography ( HPLC ). Purified PTM was successfully separated from TM , and the recovered PTM molecule was reduced with dithiothreitol to separate again by HPLC . Two subunits were obtained and peptides from each digested subunit by V8 protease were recovered by HPLC , and then amino acid sequences of the peptides were analyzed by protein sequencing. As a result, some amino acid residues were replaced from that of TM α1 isoform which is the major isoform of TM , and also was different between the two subunits. Therefore, it is concluded that PTM clearly differs from TM and it is suggested that functional difference in PTM from TM is attributed to amino acid replacements in subunits composing PTM .