Effect of acetylation on conformation and bilirubin-binding properties of goat serum albumin.
Four acetylated derivatives of goat serum albumin with percentage modifications of 18, 40, 53 and 93% were checked for bilirubin-binding and conformational properties. Acetylation caused marked changes in protein conformation, as evidenced by double immunodiffusion and proteolytic digestion results, as well as a decrease in bilirubin binding. An increase in ionic strength had a dramatic effect on the bilirubin-binding characteristics of modified proteins. The results suggest that the lysine residues of goat serum albumin modified in this study are not involved in bilirubin-albumin interaction.
Tayyab
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S
Protein and Enzyme Laboratory, Aligarh Muslim University, Uttar Pradesh, India.
Qamar
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Islam
M
M
D000107:Acetylation; D000818:Animals; D001663:Bilirubin / Q000737:chemistry / Q000378:metabolism*; D002918:Chymotrypsin; D006041:Goats; D006801:Humans; D006868:Hydrolysis; D005779:Immunodiffusion; D007231:Infant, Newborn; D007647:Kernicterus / Q000209:etiology; D046911:Macromolecular Substances; D009994:Osmolar Concentration; D011485:Protein Binding; D011487:Protein Conformation; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D014357:Trypsin
D046911:Macromolecular Substances; D012709:Serum Albumin; D002918:Chymotrypsin; D014357:Trypsin; D001663:Bilirubin