Allosteric modulation of zinc speciation by fatty acids

• Published in: Biochimica et biophysica acta Vol. 1830; no. 12; pp. 5456 - 5464
• Main Authors: Barnett, James P., Blindauer, Claudia A., Kassaar, Omar, Khazaipoul, Siavash, Martin, Esther M., Sadler, Peter J., Stewart, Alan J.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2013
• Subjects: Allosteric Regulation; Allostery; binding sites; blood plasma; Circulation; diabetes; drugs; fatty acids; Fatty Acids - blood; Fatty Acids - chemistry; hormones; Humans; Ion Transport; ligands; metal ions; Models, Molecular; myocardial ischemia; Protein Binding; Protein–lipid interaction; Protein–metal interaction; Serum albumin; Serum Albumin - chemistry; Serum Albumin - metabolism; Zinc; Zinc - blood; Zinc - chemistry; ACB; FA1–7; HRR; Allostery; Serum albumin; EXAFS; Zinc; Protein–metal interaction; mol. eq; BSA; ATCUN; TCA; HSA; ITC; HRG; IMA; MI; Protein–lipid interaction; Circulation; histidine-rich glycoprotein; ischemia-modified albumin; histidine-rich region; fatty acid-binding sites 1–7; isothermal titration calorimetry; amino-terminal copper and nickel binding; tricarboxylic acid; molar equivalents; albumin-cobalt-binding; extended X-ray absorption spectroscopy; myocardial ischemia; human serum albumin; bovine serum albumin
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2013.05.028

Serum albumin is the major protein component of blood plasma and is responsible for the circulatory transport of a range of small molecules that include fatty acids, hormones, metal ions and drugs. Studies examining the ligand-binding properties of albumin make up a large proportion of the literatur...