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1. Mutation Screen Of "Gamma-Aminobutyric Acid (Gaba)-A Receptor, Gamma 2" In Punjab Population

by Muhammad Javed Iqbal | Dr. Muhammad Wasim | Dr. Abu Saeed | Dr. Ali Raza Awan.

Material type: book Book; Format: print ; Literary form: drama Publisher: 2012Dissertation note: Epilepsy is a formidable form of neural disorder that can impose its long lasting effect on person's life and development. To date, it lacks any effective therapy and is multistep disease strengthened by an overwhelming number of genetic and epigenetic mechanisms that streamline epileptic attacks. This particular study encompasses two major types of epilepsy, CAE and GTCS by targeting a GABRG2 gene. Mutation analysis of the coding exons (exon 3, 5 and 9) was performed by direct sequencing of GABRG2 in order to sought out complex biological entities in both types of epilepsies. GABRG2 is a molecule that has recently been characterized as the culprit for epileptic seizures onset. GABRG2 encodes GABA receptor that is fundamental inhibitory neurotransmitter in mammalian brain and is a ligand-gated chloride channels. This ligand-receptor coupling results in the inward shuttling of chloride ions through the channels and this hyperpolarizes the neurons, which induce the inhibitory effect of neurotransmitters. Direct sequencing of candidate gene "GABRG2" traced out a single polymorphic site in the exon 3 of the CAE as well as GTCS cases. However, this single nucleotide alteration is more commonly identified in childhood absence epilepsy patients as compared to the generalized cases. Silent mutation was identified at locus 27909 C>T of 46.66% of the total screened or analyzed cases. Availability: Items available for loan: UVAS Library [Call number: 1500,T] (1).

2. Production, Purification & Characterization Of Recombinant Thermostable Phytase And Its Biological Evaluation In Broiler Chicks

by Furqan Sabir (2007-VA-524) | Dr. Muhammad Tayyab | Dr. Abu Saeed Hashmi | Dr. Ali Raza Awan.

Material type: book Book; Literary form: not fiction Publisher: 2017Dissertation note: Phytate is the principle storage form of phosphorus in plants particularly in cereal grains and legumes. Mono-gastric animals doesn’t have ability to utilize phytate as phosphorus source. The animals release the undigested phytate from body with manure that cause environmental pollution. Phytases are responsible for the hydrolysis of phytate, resulting in availability of free phosphorus for the animal. The present study deals with the production and characterization of recombinant thermostable phytase and its biological evaluation in the broiler chicks. The PCR resulted in the amplification of 1.8 kb phytase gene using the genomic DNA of Thermotoga naphthophila as template. The purified PCR product was ligated in pTZ57R/T and the ligated material was utilized for the transformation of E.coli DH5α cells. The positive clones were selected on the basis of blue white screening. The restriction digestion of plasmid DNA from positive clones using NdeI and Hind III resulted in the release insert from the vector. The purified phytase gene after restriction digestion was ligated into pET21a already restricted with the same restriction enzymes and the expression was analyzed using E.coli BL21 CodonPlus (DEL) cells. SDS-PAGE demonstrated the intra-cellular production of recombinant phytase. The conditions were optimized for the optimal production of recombinant phytase (PHYTN). The maximal production of PHYTN was recorded when the BL21 CodonPlus cells having recombinant pET21a having phytase gene were induced with 1.4 mM IPTG and 6 hours post induction incubation period. The recombinant protein was purified using various chromatographic techniques and the purified protein was utilized for characterization. PHYTN showed optimal activity at 80 °C and pH 6 in sodium acetate buffer. The enzyme was found metal dependent and presence of Fe3+ or Cu2+ showed enhancing effect on PHYTN activity. Thermostability studies demonstrated that PHYTN retains 90% residual SUMMARY 71 activity when the protein was incubated at 80 °C for 1h in the presence of 1.5 mM Fe3+. The kinetic studies of PHYTN demonstrated km and Vmax values of 50 mM and 2500 μmole/min respectively when sodium phytate was used as substrate. The characterized PHYTN was used for poultry trials to check the efficacy of the enzyme in poultry birds. The results depicted that PHYTN put significant effect on the bird weight gain, feed intake and feed efficiency ratio. Presence of 1000 IU/kg of PHYTN resulted in the weight gain in 3rd, 4th and 5th week of trials from 504.766 to 533.535 g, 767.933 to 823.733 g and 999.833 to 1120.277 g respectively when compared with the control. The study demonstrated that this recombinant thermostable phytase is suitable for poultry feed industry and its domestic production will contribute the economic availability of PHYTN for the poultry feed industry. Availability: Items available for loan: UVAS Library [Call number: 2870-T] (1).

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