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Updated: May 27, 2026

Exploring the Longissimus Muscle: Unraveling its Correlation with Meat Quality in Bos indicus and Crossbred Bulls
Published on: July 12, 2024
Myosin heavy chain isoforms expressed in bovine skeletal muscles
K Chikuni1, S Muroya, I Nakajima
1Meat Science Laboratory, Department of Animal Products, National Institute of Livestock and Grassland Science, Norin-kenkyu-danchi, P.O. Box 5, Ikenodai 2, Tsukuba, Ibaraki 305-0901, Japan.
Abstract:
Nucleotide sequences including the full coding region for three types of myosin heavy chain (MyHC) isoforms were determined from bovine adult skeletal muscles. The deduced amino acid sequences were 1940, 1938, and 1935 residues for the MyHC-2a, -2x, and -slow, respectively. Like other mammalian MyHC isoforms, the bovine MyHC isoforms had homologous sequences except for substitutions concentrated on the loop 1, loop 2, and light chain binding regions. RT-PCR amplifications showed that the adult bovine skeletal muscles expressed the MyHC-2a, -2x, and -slow isoforms but no -2b isoform. The absence of the MyHC-2b isoform and substitutions on the loop2 region could explain some differences in meat quality between beef and pork.
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