Author/Authors :
Dinparast Djadid, Navid Pasteur Iinstitute of Iran - Biotechnology Research Center - Malaria and Vector Research Group (MVRG), تهران, ايران , Nikmard, Mehdi zanjan university - College of Agriculture - Animal Science Department, زنجان, ايران , Zakeri, Sedigheh Pasteur Iinstitute of Iran - Biotechnology Research Center - Malaria and Vector Research Group (MVRG), تهران, ايران , Gholizadeh, Saber Pasteur Iinstitute of Iran - Biotechnology Research Center - Malaria and Vector Research Group, تهران, ايران
Abstract :
Calpastatin is an endogenous inhibitor of calpain (calcium- dependent cysteine protease). Calpastatin activity is highly related to the rate of protein turnover and rate of meat tenderization. In order to characterize the structure of calpastatin in Iranian Afshari breed of sheep, intron 6 and partial exon 7 of the L domain were amplified and sequenced. A fragment of approximately 1.5 kb was identified. In this study, an Afshari calpastatin gene fragment that encoded L Domain amino acids was detected. Hence by detection of such conserved mutations, it is possible to use these polymorphisms in Marker-Assisted Selection (MAS).
Keywords :
Calpastatin , Sequence analysis , Iran , Afshari sheep
