Chemical Modification of the High-Affinity Bilirubin-Binding Site of Human-Serum Albumin

1972 ◽  
Vol 27 (3) ◽  
pp. 513-519 ◽  
Author(s):  
Christian JACOBSEN
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Chemical Modification ◽  
Human Serum ◽  
Binding Site ◽  
High Affinity ◽  
Bilirubin Binding

scholarly journals 20: Mapping of the High-Affinity Bilirubin-Binding Site of Human Serum Albumin

1976 ◽  
Vol 10 (10) ◽  
pp. 876-876
Author(s):  
N Gitzelmann-Cumarasamy ◽  
C C Kuenzle ◽  
G Duc
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
High Affinity ◽  
Bilirubin Binding

Identification and Characterization of a Single High-Affinity Fatty Acid Binding Site in Human Serum Albumin

2017 ◽  
Vol 130 (4) ◽  
pp. 1056-1060 ◽  
Author(s):  
Lea Wenskowsky ◽  
Herman Schreuder ◽  
Volker Derdau ◽  
Hans Matter ◽  
Julia Volkmar ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Fatty Acid Binding ◽  
High Affinity ◽  
Identification And Characterization ◽  
Fatty Acid Binding Site

Identification and Characterization of a Single High-Affinity Fatty Acid Binding Site in Human Serum Albumin

2017 ◽  
Vol 57 (4) ◽  
pp. 1044-1048 ◽  
Author(s):  
Lea Wenskowsky ◽  
Herman Schreuder ◽  
Volker Derdau ◽  
Hans Matter ◽  
Julia Volkmar ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Fatty Acid Binding ◽  
High Affinity ◽  
Identification And Characterization ◽  
Fatty Acid Binding Site

scholarly journals Spectroscopic investigations on the binding of an iodinated chlorin p6-copper complex to human serum albumin

2017 ◽  
Vol 16 (12) ◽  
pp. 1762-1770 ◽  
Author(s):  
P. Sarbadhikary ◽  
A. Dube
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Copper Complex ◽  
Protein Conformation ◽  
High Affinity ◽  
Spectroscopic Investigations ◽  
Chlorin P6

An iodinated chlorin p6 copper complex showed high affinity to bind human serum albumin, the binding site was predicted and it was demonstrated that binding did not affect protein conformation.

scholarly journals Dansylation of human serum albumin in the study of the primary binding sites of bilirubin and l-tryptophan

1979 ◽  
Vol 181 (1) ◽  
pp. 251-253 ◽  
Author(s):  
C Jacobsen ◽  
J Jacobsen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Sites ◽  
Lysine Residue ◽  
Bilirubin Binding ◽  
Albumin Molecule ◽  
Common Cavity

Binding of bilirubin and of L-tryptophan to dansylated albumins was investigated. Dansylation of less than one lysine residue per molecule of albumin did not affect the bilirubin binding, but decreased the L-tryptophan binding, indicating that dansylation had taken place in or near the l-tryptophan-binding site. Native albumin and albumin-bilirubin 1:1 complex showed the same affinity for L-tryptophan. The results indicate that, although L-tryptophan and bilirubin are bound in the same region, perhaps in a common cavity of the albumin molecule, such a cavity is sufficiently large to contain both ligands.

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