We are grateful to Prof. K. Takahashi of the Faculty of Agriculture, University of Hokkaido, Japan, for valuable comments.
Skeletal Muscle Connectin Primary Structures as Related to Animal Species and Muscle Type
Article first published online: 20 JUL 2006
Journal of Food Science
Volume 62, Issue 3, pages 451–453, May 1997
How to Cite
TANABE, R., MUROYA, S., NAKAJIMA, I., CHIKUNI, K. and NAKAI, H. (1997), Skeletal Muscle Connectin Primary Structures as Related to Animal Species and Muscle Type. Journal of Food Science, 62: 451–453. doi: 10.1111/j.1365-2621.1997.tb04404.x
- Issue published online: 20 JUL 2006
- Article first published online: 20 JUL 2006
- Ms received 7/8/96; revised 10/21/96; accepted 10/29/96.
- skeletal muscle;
- meat texture;
- meat conditioning
Differences in molecular weights and partial amino acid sequences of connectin(titin) were determined for cattle, pig and chicken skeletal muscles. Peptide mapping analysis results differed according to animal species. Amino acid sequences deduced from partial nucleotide sequences of connectin also differed according to animal species at immunoglobulin-like (Ig) and fibronectin type 3 (FN3) domains. In chicken, the molecular weight of connectin from leg muscles was higher than that from pectoral muscles. Differences in meat texture and conditioning may relate to connectin and extent of its breakdown.