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Effect of Biochemical Polymorphisms on Performance Traits in Indigenous Chicken Genotypes

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Effect of Biochemical Polymorphisms on Performance Traits in Indigenous Chicken Genotypes.


This research investigated the effect of biochemical polymorphisms on performance traits in Nigerian indigenous chicken genotypes. The chickens were obtained from pedigree mating of Normal feathered, Frizzle feathered and Naked Neck cocks to Normal feathered, Frizzle feathered and Naked Neck hens respectively to produce F1 offspring. One hundred and fifty-five chicks (37 Frizzle, 79 Normal and 39 Naked Neck) were measured for body weight (g), breast girth (cm) and tibia length (cm).

At 20weeks, 5ml of blood was collected from wing vein of each chicken into heparinized tubes labeled according to its tag number for electrophoresis. Each bird was scored as either fast (AA), midway (AB) or slow (BB) according to the mobility on the cellulose-acetate paper for each of transferrin, haemoglobin and carbonic anhydrase. Data obtained were subjected to general linear model procedure of statistical analysis system (SAS, 2002) and significant means were separated using tukey honestly significant difference.

Hardy Weinberg‟s equation was used to calculate genotypic and allelic frequencies and tested using chi-square (χ2). Each of the three biochemical markers distinguished into three polymorphic forms viz; AA, AB and BB. The Frizzle feathered had significant higher (P<0.05) weight (338.54g) than both the Normal feathered (319.59g) and Naked Neck (295.51g) from day old to 8weeks, with no significant differences (P>0.05) from 12 to 20 weeks with no consistent trend for tibia length and breast girth.

The effect of sexual dimorphism was significant (P<0.05) with males having significantly higher body weight (1168.79g) than females (937.06g), breast girth, males (25.74cm) and females (24.24cm) and tibia length, males (9.59cm) and females (8.96cm). The genotypic frequencies of Transferrin (TfAATfAB and TfBB) had 8, 140 and 7 respectively, haemgolobin (HbAAHbAB and HbBB), had 49, 56 and 50 respectively and carbonic anhydrase (CaAACaAB and CaBB) had 63, 79 and 13 respectively.


The local breeds of chicken also referred to as indigenous chickens are genetically adapted to harsh environment facing limited resources and severe challenges from climatic conditions, pathogens and predators (Mwacharo et al., 2005; Sorenson, 2009). They are often utilized for several purposes simultaneously (Sorenson, 2009; Adeleke et al., 2011a), and possess both superior levels of genetic diversity/variation relative to commercial breeds (which have been selected for a particular performance traits) and they have unique traits of valuable local adaptations (Sorenson, 2009).

Some local chickens have special characteristics of potential interest to commercial breeders. Therefore, indigenous chickens could be genetic source for future breeding strategies (Horst, 1999). Genetic or protein polymorphism results from variations in the proteins or specifically in the amino acids for which the same genes code in different individuals, strains, breeds (Rege and Okeyo, 2006; Kwaga, 2006). This is the occurrence of two or more discontinuous forms of protein in a species/population in such a proportion that the rarest phenotype which has a frequency of more than 0.1 percent cannot be maintained merely by recurrent mutation (Das and Deb, 2008).

Protein polymorphism can be used to map (locate) genes such as those causing a disease, for economic traits, selection of superior animals for breeding purposes (Akpa et al., 2011) and they can help match two samples of deoxyribonucleic acid (DNA) to determine if they come from the same source. In general, this variation in proteins can be used for the study of genetic diversity within a population‟s gene pool by applying two approaches viz; protein electrophoresis and protein immunology, bearing in mind that the basic principle behind electrophoretic mobility of enzymes as well as other proteins is mobility across gels, which denotes differences in allelic groups responsible for amino acid variations in the protein (Rege and Okeyo, 2006). 


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CSN Team.

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