R. Tanabe et al., SKELETAL-MUSCLE CONNECTIN PRIMARY STRUCTURES AS RELATED TO ANIMAL SPECIES AND MUSCLE-TYPE, Journal of food science, 62(3), 1997, pp. 451
Differences in molecular weights and partial amino acid sequences of c
onnectin(titin) were determined for cattle, pig and chicken skeletal m
uscles. Peptide mapping analysis results differed according to animal
species. Amino acid sequences deduced from partial nucleotide sequence
s of connectin also differed according to animal species at immunoglob
ulin-like (Ig) and fibronectin type 3 (FN3) domains. In chicken, the m
olecular weight of connectin from leg muscles was higher than that fro
m pectoral muscles. Differences in meat texture and conditioning may r
elate to connectin and extent of its breakdown.