noor fazielawanie - Academia.edu (original) (raw)
Papers by noor fazielawanie
Fish Physiology and Biochemistry, 2012
A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellog... more A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellogenin (vtg). Two-year-old juvenile L. calcarifer (n = 10) were given three intraperitoneal injections of 17-β estradiol (E2) at a dose of 2 mg/kg body weight to induce vitellogenesis. Blood was collected 3 days after the last injection, and plasma was purified through gel filtration chromatography. A broad single symmetrical peak consisting of vtg molecule was produced. Protein concentration was 0.059 mg/ml as determined by Bradfrod assay using bovine serum albumin as a standard. The protein appeared as one circulating form in Native PAGE considering the dimeric form of putative vtg with molecular weight of 545 kDa. In SDS-PAGE under reducing conditions, two major bands appeared at 232.86 and 118.80 kDa and minor bands at 100.60, 85.80 and 39.92 kDa, respectively. The purified vtg was used to generate a polyclonal antibody, and the specificity of antibody was assessed by Western blot analysis. Two major bands were immunoreacted, but no cross-reactivity was observed with plasma from non-induced males. The protein was characterized as phosphoglycolipoprotein as it positively stained for the presence of lipid, phosphorus and carbohydrate using Sudan Black B, methyl green and periodic acid/Schiff reagent solution, respectively. The amino acid composition was analyzed by high sensitivity amino acid analysis that showed high percentage of non-polar amino acids (~48 %). The results suggest the potential utilization of vtg as a basis tool to further study about reproductive physiology of this important economical species.
Fish Physiology and Biochemistry, Aug 10, 2012
A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellog... more A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellogenin (vtg). Two-year-old juvenile L. calcarifer (n = 10) were given three intraperitoneal injections of 17-β estradiol (E 2) at a dose of 2 mg/kg body weight to induce vitellogenesis. Blood was collected 3 days after the last injection, and plasma was purified through gel filtration chromatography. A broad single symmetrical peak consisting of vtg molecule was produced. Protein concentration was 0.059 mg/ml as determined by Bradfrod assay using bovine serum albumin as a standard. The protein appeared as one circulating form in Native PAGE considering the dimeric form of putative vtg with molecular weight of 545 kDa. In SDS-PAGE under reducing conditions, two major bands appeared at 232.86 and 118.80 kDa and minor bands at 100.60, 85.80 and 39.92 kDa, respectively. The purified vtg was used to generate a polyclonal antibody, and the specificity of antibody was assessed by Western blot analysis. Two major bands were immunoreacted, but no cross-reactivity was observed with plasma from non-induced males. The protein was characterized as phosphoglycolipoprotein as it positively stained for the presence of lipid, phosphorus and carbohydrate using Sudan Black B, methyl green and periodic acid/Schiff reagent solution, respectively. The amino acid composition was analyzed by high sensitivity amino acid analysis that showed high percentage of non-polar amino acids (~48 %). The results suggest the potential utilization of vtg as a basis tool to further study about reproductive physiology of this important economical species.
Vitellogenin (vtg) is a major protein present abundantly in female fish undergoing oogenesis. In ... more Vitellogenin (vtg) is a major protein present abundantly in female fish undergoing oogenesis. In male and immature fish, vtg gene is normally suppressed. However, vtg synthesis can be induced by administration of estrogen hormone (E2). This study was conducted to induce, purify and characterize vtg in E2-treated immature Lates calcarifer. This is important for screening maturity status of this economically important species in a farm. Two-year old immature L. calcarifer (n=10) were given three intraperitoneal injections of 17-β estradiol (E2) at a dose of 2 mg/kg body weight at two days intervals to induce vitellogenesis. Control groups (vitellogenic female and matured male L. calcarifer, n=6) were injected with 0.9% saline only. Blood was collected three days after the last injection and plasma was purified through gel filtration chromatography using Sepachryl HR-300 column, eluted with Tris-HCl pH 8.0. A broad, single symmetrical peak consisting of vtg molecule was produced. Prote...
Fish Physiology and Biochemistry, 2012
A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellog... more A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellogenin (vtg). Two-year-old juvenile L. calcarifer (n = 10) were given three intraperitoneal injections of 17-β estradiol (E2) at a dose of 2 mg/kg body weight to induce vitellogenesis. Blood was collected 3 days after the last injection, and plasma was purified through gel filtration chromatography. A broad single symmetrical peak consisting of vtg molecule was produced. Protein concentration was 0.059 mg/ml as determined by Bradfrod assay using bovine serum albumin as a standard. The protein appeared as one circulating form in Native PAGE considering the dimeric form of putative vtg with molecular weight of 545 kDa. In SDS-PAGE under reducing conditions, two major bands appeared at 232.86 and 118.80 kDa and minor bands at 100.60, 85.80 and 39.92 kDa, respectively. The purified vtg was used to generate a polyclonal antibody, and the specificity of antibody was assessed by Western blot analysis. Two major bands were immunoreacted, but no cross-reactivity was observed with plasma from non-induced males. The protein was characterized as phosphoglycolipoprotein as it positively stained for the presence of lipid, phosphorus and carbohydrate using Sudan Black B, methyl green and periodic acid/Schiff reagent solution, respectively. The amino acid composition was analyzed by high sensitivity amino acid analysis that showed high percentage of non-polar amino acids (~48 %). The results suggest the potential utilization of vtg as a basis tool to further study about reproductive physiology of this important economical species.
Fish Physiology and Biochemistry, Aug 10, 2012
A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellog... more A study was conducted to isolate, partial characterize Asian sea bass (Lates calcarifer) vitellogenin (vtg). Two-year-old juvenile L. calcarifer (n = 10) were given three intraperitoneal injections of 17-β estradiol (E 2) at a dose of 2 mg/kg body weight to induce vitellogenesis. Blood was collected 3 days after the last injection, and plasma was purified through gel filtration chromatography. A broad single symmetrical peak consisting of vtg molecule was produced. Protein concentration was 0.059 mg/ml as determined by Bradfrod assay using bovine serum albumin as a standard. The protein appeared as one circulating form in Native PAGE considering the dimeric form of putative vtg with molecular weight of 545 kDa. In SDS-PAGE under reducing conditions, two major bands appeared at 232.86 and 118.80 kDa and minor bands at 100.60, 85.80 and 39.92 kDa, respectively. The purified vtg was used to generate a polyclonal antibody, and the specificity of antibody was assessed by Western blot analysis. Two major bands were immunoreacted, but no cross-reactivity was observed with plasma from non-induced males. The protein was characterized as phosphoglycolipoprotein as it positively stained for the presence of lipid, phosphorus and carbohydrate using Sudan Black B, methyl green and periodic acid/Schiff reagent solution, respectively. The amino acid composition was analyzed by high sensitivity amino acid analysis that showed high percentage of non-polar amino acids (~48 %). The results suggest the potential utilization of vtg as a basis tool to further study about reproductive physiology of this important economical species.
Vitellogenin (vtg) is a major protein present abundantly in female fish undergoing oogenesis. In ... more Vitellogenin (vtg) is a major protein present abundantly in female fish undergoing oogenesis. In male and immature fish, vtg gene is normally suppressed. However, vtg synthesis can be induced by administration of estrogen hormone (E2). This study was conducted to induce, purify and characterize vtg in E2-treated immature Lates calcarifer. This is important for screening maturity status of this economically important species in a farm. Two-year old immature L. calcarifer (n=10) were given three intraperitoneal injections of 17-β estradiol (E2) at a dose of 2 mg/kg body weight at two days intervals to induce vitellogenesis. Control groups (vitellogenic female and matured male L. calcarifer, n=6) were injected with 0.9% saline only. Blood was collected three days after the last injection and plasma was purified through gel filtration chromatography using Sepachryl HR-300 column, eluted with Tris-HCl pH 8.0. A broad, single symmetrical peak consisting of vtg molecule was produced. Prote...