Isolation, purification and advanced characterization of hormone inhibin in ovary of female camel are aimed in this study. Pooled follicular fluid was collected from the ovaries of she-camel irrespective to physiological status and age of the animals.  Follicular fluid was subjected to 2 types of gel filtration chromatography; Sephacryl S-200 where three peaks of proteins was obtained.  The suspected peak to contain inhibin (peak III) resolved from S-200 was subjected to Sephadex G-100 where three peaks were obtained, third peak was suspected to contain inhibin in pure form. To verify the purity of the isolated hormone, the lyophilized fraction containing inhibin was subjected to analysis by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under both non reducing condition, stained with silver nitrate where a single band was resolved, and under reducing condition, where five bands resolved (ranging between 58.8 to 32.3 KDa). Using Reversed Phase-High Performance Liquid Chromatography (RP-HPLC) to fractionate the third peak, subunits of inhibin hormone eluted at different retention times. High Performance-Thin Layer Chromatography (HP-TLC) used to determine the N-terminal amino acids contents of the third peak and  7 amino acids resolved with different concentrations where histidine was the most abundant of the amino acids.