Biochemical characterization of inhibin hormone in the ovary of she camel (Camelus dromedaries) [electronic resource].

By: Contributor(s): Language: English Summary language: Arabic Description: p.1-18Other title:
  • التعرف على هرمون الانهبين في مبايض إناث الجمال باستخدام الطريقة الكيميائية الحديثة [Added title page title]
Uniform titles:
  • Assiut veterinary medical journal, 2007 v. 53 (112) [electronic resource].
Subject(s): Online resources: In: Assiut Veterinary Medical Journal 2007.v.53(112)Summary: 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 ofshe-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 0-100 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-PAOE) 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 PhaseHigh 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 ofthe amino acids.
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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 ofshe-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 0-100 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-PAOE) 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 PhaseHigh 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 ofthe amino acids.

Summary in Arabic.

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