Saurabh Vaishnav1, Wahiduzzaman2, Faizan Ahmad2, Md. Imtaiyaz Hassan2
1Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025; Amity Institute of Biotechnology, Amity University, NOIDA, UP, India.
2Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, India.

ABSTRACT

Kidney contains higher concentration of Annexin A4 due to the fact that it has major role in the membrane transport and osmoregulation. It also exhibits calcium dependent phospholipid binding activity and differentially binds both phospholipid and carbohydrates. We have first time purified Annexin A4 from goat kidney which was found to be present in the form of complex with Fc region of immunoglobulin G (Ig-G), to the highest purity. The 30-60% ammonium sulphate precipitation fraction goat kidney homogenate was applied to cation exchange chromatography on CM-Sephadex C-50 in 50 mM sodium acetate buffer (pH 5.0). The eluted fraction was analyzed and the band of Annexin A4 was visible at 33 KDa along with a 14 KDa band on reducing SDS-PAGE. The two proteins were eluted together on Sephacryl S100 column in a single peak revealed that both proteins are forming a complex. The 33 kDa and 14 kDa bands on SDS-PAGE was identified as Annexin A4 and Fc region of Ig-G, respectively. This is first report on the isolation, purification and characterization of a naturally occurring complex of Annexin A4 with the Fc fragment of Ig-G. Read more…

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