Journal of Biotechnology & Biomaterials
Open Access

Abstract

Inhibins are multifunctional molecules involved in the control of pituitary FSH secretion. Inhibins are glycoprotein hormones produced in the gonads and are capable of regulating FSH secretion by the pituitary gland. Inhibins show a reciprocal relationship with FSH during estrous cycle. Immunization against inhibin enhances FSH secretion and follicular growth and fi nally increases the ovulation rate. Th e present research work was envisaged with cloning, expression and biological characterization of recombinant inhibin protein. Th e bovine inhibin-alpha immunogenic region of about 404 base pairs region representing carboxylterminal end of second exon was amplifi ed, cloned and expressed in prokaryotic host. Purifi cation of recombinant protein was achieved by Ni-NTA column. Th e protein was immunologically characterized by ELISA, Dot-blot and Western blotting. Th e biological effi cacy of recombinant bovine inhibin-alpha was tested in guinea pigs for fecundity augmentation. Two diff erent doses of recombinant inhibin (10 �¼g and 25 �¼g) along with adjuvants were administered to various experimental groups. Th e percentage of pregnant guinea pigs varied from 60%-100%. Th e number of litters born aft er treatment with recombinant bINH-�± was between 2.14 to 2.75. Since, there was non-normal distribution of data, Mann-Whitney test was employed. Th e average number of litter size born in experimental groups compared to control group was found to be increased. No signifi cant change in ovulation/litter size was observed between the control group 0 (without recombinant bINH-�± administration) and the group 1 (with 10 �¼g recombinant bINH-�± administration). However, the increase in ovulation/litter size between the control group 0 and the treatment group 2 (with 25 �¼g recombinant bINH-�± administration) was found to be highly signifi cant (P â�¤ 0.05).

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