अमूर्त

Determination of Riboflavin Binding Protein (Rfbp) in SDS /Native PAGE Electrophoresis

M. Bapu Rao, M.Vijay Kumar and G.Rajender


Riboflavin binding protein (Rfbp) was isolated from Hen (Gallus gallus) and Peacock(Pavo cristatus) egg-white, egg-yolk. The protein was purified in two steps, DEAE-Sephadex A-50 ion exchange chromatography. The protein was eluted with phosphate buffer pH 7.3 containing 0.5 M sodium chloride. The final purification of protein was achieved on sephadex G-100. Collected Protein fractions were determined by the method of Lowry. Absorbance was measured at 280 nm and 455 nm using UV-visible spectrophotometer. The purity of the protein was judged on cylindrical and slab gel electrophoresis, SDS (Sodium do-doceyl sulphate)-PAGE (Poly acrylamide gel electrophoresis) technique.Sephadex G-100 fraction Rfbp moved as a single band both on the Slab and Cylindrical gels .Comparison of the mobility of Rfbp with that of the standard molecular weight marker proteins revealed with that the Rfbp had a molecular weight close to 29,000 kilodaltons.Interestingly, hen egg-white Rfbp and peacock egg- white, yolk Rfbp had the same molecular weight as revealed by the SDS polyacrylamide gel electrophoresis.


अस्वीकृति: इस सारांश का अनुवाद कृत्रिम बुद्धिमत्ता उपकरणों का उपयोग करके किया गया है और इसे अभी तक समीक्षा या सत्यापित नहीं किया गया है।

में अनुक्रमित

  • कैस
  • गूगल ज्ञानी
  • जे गेट खोलो
  • चीन राष्ट्रीय ज्ञान अवसंरचना (सीएनकेआई)
  • उद्धरण कारक
  • ब्रह्मांड IF
  • इलेक्ट्रॉनिक जर्नल्स लाइब्रेरी
  • रिसर्च जर्नल इंडेक्सिंग की निर्देशिका (डीआरजेआई)
  • गुप्त खोज इंजन लैब्स
  • आईसीएमजेई

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