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Changes in degradation and phosphorylation level of titin in three ovine muscles during postmortem
Author(s) -
Wang Ying,
Li Xin,
Li Zheng,
Li Meng,
Zhu Jie,
Zhang Dequan
Publication year - 2018
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.13663
Subject(s) - titin , sarcomere , myofibril , phosphorylation , chemistry , protein degradation , degradation (telecommunications) , anatomy , andrology , biochemistry , medicine , biology , myocyte , telecommunications , computer science
Summary The objective of this study was to investigate the degradation of titin and its phosphorylation level in three muscles from sheep. The MFI and pH from the longissimus lumborum ( LL ), semimembranosus ( SM ) and psoas major ( PM ) muscles were measured at 30 min, 1, 2, 7, 14, 21 and 28 days postmortem. Myofibrillar proteins were extracted, separated by SDS ‐ PAGE and quantified by phosphor‐specific staining. Phosphorylation of titin was predicted by Pro‐Q Diamond‐ SYPRO Ruby staining. Two days after exsanguination, the pH and MFI of the PM were higher than those of the LL and SM muscles ( P < 0.05). The sarcomere length of the PM muscle was also longer than that of the LL and SM muscle ( P < 0.05). PM muscles had a highest phosphorylation level ( P < 0.05) at 0.5 h postmortem and showed the greatest degree of titin degradation over 28 days. This suggests that phosphorylation of titin might accelerate its degradation.