Biochemical Properties | composed of two polypeptides, the A and B
chains, and shares a high degree of amino acid identity
with fetuin; mouse AHSG
shares 60% and 65% amino acid identity with human
AHSG and bovine fetuin; A and B chains of human AHSG, held together by
a disulfide bond, are generated by limited proteolysis at Arg-Thr, equivalent position at bovine
fetuin sequence is Pro-lie |
---|
Bibliography | 1. Yang, F., Chen, Z. L., Bergeron, J. M., Cupples, R. L., & Friedrichs, W. E. (1992). Human alpha 2-HS-glycoprotein/bovine fetuin homologue in mice: identification and developmental regulation of the gene. Biochimica et Biophysica Acta, 1130(2), 149–156. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1373325. Watzlawick, H., Walsh, M. T., Yoshioka, Y., Schmid, K., & Brossmer, R. (1992). Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases. Biochemistry, 31(48), 12198–12203. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/1457416. 3. Strieder-Barboza, C., de Souza, J., Raphael, W., Lock, A. L., & Contreras, G. A. (2018). Fetuin-A: A negative acute-phase protein linked to adipose tissue function in periparturient dairy cows. Journal of Dairy Science, 101(3), 2602–2616. https://doi.org/10.3168/jds.2017-13644. |