Site-Selective Labeling of a Lysine Residue in Human Serum Albumin

2014 ◽  
Vol 126 (44) ◽  
pp. 11977-11980 ◽  
Author(s):  
Shigehiro Asano ◽  
James T. Patterson ◽  
Thomas Gaj ◽  
Carlos F. Barbas
2014 ◽  
Vol 53 (44) ◽  
pp. 11783-11786 ◽  
Author(s):  
Shigehiro Asano ◽  
James T. Patterson ◽  
Thomas Gaj ◽  
Carlos F. Barbas

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.


2021 ◽  
Vol 148 ◽  
pp. 111927
Author(s):  
Chunlei Zhu ◽  
Fengru Liu ◽  
Yunlong Wei ◽  
Fan Zhang ◽  
Ting Pan ◽  
...  

2010 ◽  
Vol 11 (1) ◽  
pp. 106-112 ◽  
Author(s):  
Yan-Jun Hu ◽  
Yu Ou-Yang ◽  
Chun-Mei Dai ◽  
Yi Liu ◽  
Xiao-He Xiao

2018 ◽  
Vol 107 ◽  
pp. 1414-1421 ◽  
Author(s):  
Mohammad Siddiqi ◽  
Saima Nusrat ◽  
Parvez Alam ◽  
Sadia Malik ◽  
Sumit Kumar Chaturvedi ◽  
...  

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