Document Type : Original Article


1 Cell Biology Department, National Res. Center, Dokki, Egypt

2 Zoology Department, Fac. of Science, Zagazig Univ., Egypt


Calpain is a ubiquitous cytoplasmic cysteine protease, its activity is dependent on calcium. Two genes of calpain- CAPN1 (µ-calpain) and CAPN2 (m-calpain) have been identified. The micromolar calcium-activated neutral protease (CAPN1) gene encodes a cysteine protease, µ-calpain that degrades myofibril proteins under postmortem conditions and appears to be the primary enzyme in the postmortem tenderization process. Regulation of µ-calpain activity has correlated with variation in meat tenderness. Genetic polymorphism analysis of CAPN1 gene would likely aid in the development of selection criteria for improving meat tenderness. This study aimed to detect genetic polymorphism within intron 14 of buffalo CAPN1 gene using PCR-RFLP technique.
Buffalo DNA was amplified using primers that were designed from the cattle CAPN1 gene sequence. The amplified fragments obtained from all tested buffalo DNA (100 animals) at 670-bp were digested with FokI endonuclease. All buffalo animals are genotyped as CC where all tested buffalo DNA amplified fragments were digested with FokI endonuclease and gave two digested fragments at 530-bp and 140-bp due to the presence of C base at position 4685 in all tested animals and the absence of T base in this position within intron 14.


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