@article{oai:rakuno.repo.nii.ac.jp:00001299,
 author = {Lee, Eun-Jung and Kim, Young-Ho and Lee, Nam-Hyouck and Hong, Suk-In and Yamamoto, Katsuhiro and Kim, Yun-Ji},
 issue = {3},
 journal = {Meat Science},
 month = {Mar},
 note = {Article, To observe the role of sarcoplasmic protein (SP) on myofibrillar protein (MP) denaturation under a hydrostatic pressure (HP), MP isolated from bovine muscle was treated with 300 MPa by increasing concentrations of SP (0, 0.8, 1.6, and 3.2 mg/ml) from bovine. SDS-PAGE patterns of soluble proteins in 0.1 M NaCl (pH 7.4) indicated that a protein (about 100 kDa) from MP decreased with increasing concentrations of SP and that a 97 kDa protein from SP observed with 0.1 MPa was not observed with 300 MPa. SDS-PAGE patterns of soluble proteins in 0.6 M NaCl (pH 7.4) and Ca-ATPase activity showed that the denaturation of myosin heavy chain (MHC) was accelerated with increasing SP concentrations with the 300 MPa treatment. Thus, the addition of SP enhanced HP-induced denaturation of MHC and of a protein from MP of about 100 kDa.},
 pages = {219--222},
 title = {The role of sarcoplasmic protein in hydrostatic pressure-induced myofibrillar protein denaturation},
 volume = {87},
 year = {2011}
}