Abstract

  In modern programs of animal breeding, the genetic polymorphisms of production traits can be used as marker systems. Calpastatin gene is located on ovine chromosome 5 and is polymorphic in many breeds of sheep. Calpastatin has a role in meat tenderness after slaughter. Blood samples were collected from 120 crossbreeds of Dalagh sheep located in Golistan province of Iran. Genomic DNA was extracted from blood sample. Gel monitoring and spectrophotometer methods were used to determine the quality and quantity of DNA. Intron I from L domain of the ovine calpastatin gene was amplified to produce a 565 bp fragment. The PCR products were digested by restriction endonucleases MspI. Digested products were separated by electrophoresis on 1.5% agarose gel and visualized after staining with ethidium bromide on UV transillumination. The MspI digestion of the PCR products produced digestion fragments of 306 and 259 bp. Data analysis was done using PopGen32 software. In this population, MM, MN and NN genotype were identified with 65.5, 29, 5.5% frequencies, respectively. The population was found to follow Hardy-Weinberg equilibrium.   Key words: Calpastatin gene, polymorphism, crossbreed, Dalagh sheep.

Highlights

  • Genetic polymorphism in native breeds is a major concern when considering the necessity of preserving genetic resources

  • Blood samples were collected from 120 crossbreeds of Dalagh sheep located in Golistan province of Iran

  • Increased rate of skeletal muscle growth can result from a decreased rate of muscle protein degradation, and this is associated with a decrease in activity of the calpain system, due principally to a large increase in calpastatin activity (Goll et al.,1998)

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Summary

Introduction

Genetic polymorphism in native breeds is a major concern when considering the necessity of preserving genetic resources. Calpastatin, which is an endogenous inhibitor (Ca2+ dependent cysteine proteinase), plays a central role in regulation of calpain activity in cells (Murachi et al, 1981; Murachi, 1983; Forsberg et al, 1989) and is considered as one of the major modulators of the calpain. The N-terminal leader (L) domain does not appear to have any calpains inhibitory activity (Figure 1), but maybe involved in targeting or intracellular localization (Takano et al, 1999), while the other domains (I-IV) are highly homologous and are each independently capable of inhibiting calpains (Cong et al, 1998).

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