Abstract—α2-μ-Globulin fragment (A2-f) functions as a fatty acid binding protein in kidneys of male rats. It has 100% sequence homology with amino acids 10-160 of α2-μ-Globulin (A2), an 18.6-kDa protein that is synthesized in male rat liver and is present in urine. A2-f is produced from A2 by the removal of 3 residues from the N-terminus and 9 amino acids residues from the C-terminus. This project aimed to isolate and purify A2-f (to >90% purity) for NMR analysis since the solution state structure of A2-f is still unknown. The purification failed due to formation of multimers in vitro but it did reveal heterogeneity of this protein as isolated from tissue.

Index Terms—2-μ-Globulin fragment (A2-f), 2-μ-Globulin (A2), kidney fatty acid binding protein, Lipocalins, protein aggregation, male rat urinary proteins.

Abdul Hai and Nadeem A. Kizilbash are with the Department of Biochemistry, Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar-91431, Saudi Arabia (e-mail: synavia@gmail.com, fsd707@ gmail.com).
Jamal Alruwaili is with Faculty of Medicine & Applied Medical Sciences, Northern Border University, Arar-91431, Saudi Arabia (e-mail: malkh1195@hotmail.com).

 

Cite: Abdul Hai, Nadeem A. Kizilbash, and Jamal Alruwaili, "α2-μ-Globulin Fragment (A2-f) from Kidneys of Male Rats forms Multimers in Vitro," International Journal of Bioscience, Biochemistry and Bioinformatics vol. 4, no. 2, pp. 121-124, 2014.