Role of salt bridge(s) in the binding and photoconversion of bilirubin bound to high affinity site on human serum albumin

Author(s):  
Mohd.Mushahid Khan ◽  
Salman Muzammil ◽  
Saad Tayyab
1978 ◽  
Vol 171 (2) ◽  
pp. 453-459 ◽  
Author(s):  
C Jacobsen

Bilirubin can be coupled covalently to albumin by using water-soluble carbodi-imide as coupling reagent. The optimal specificity in the attachment of bilirubin to the high-affinity site on the albumin molecule was obtained by treating an albumin-bilirubin complex with carbodi-imide in low concentrations and for a short period. The product was reduced, carboxymethylated and digested with trypsin. By fractionation on Sephadex G-50 (superfine grade) a peptide fraction containing most of the bilirubin label was isolated. Further purification by paper chromatography gave one peptide, consisting of residues 240-258. The peptide containined a single lysine residue, 240, and had an intact disulphide bridge. The results indicate that bilirubin is bound to lysine residue 240 at its high-affinity site on human serum albumin.


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...  

FEBS Journal ◽  
2011 ◽  
Vol 278 (21) ◽  
pp. 4100-4111 ◽  
Author(s):  
Ai Minomo ◽  
Yu Ishima ◽  
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...  

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Kabir-ud-Din

Toxicon ◽  
2019 ◽  
Vol 168 ◽  
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