Expression of a Human Serum Albumin Variant with High Affinity for Thyroxine

1995 ◽  
Vol 214 (3) ◽  
pp. 1121-1129 ◽  
Author(s):  
C.E. Petersen ◽  
C.E. Ha ◽  
M. Mandel ◽  
N.V. Bhagavan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
High Affinity ◽  
Albumin Variant

scholarly journals Biological characteristics of two lysines on human serum albumin in the high-affinity binding of 4Z,15Z-bilirubin-IXα revealed by phage display

FEBS Journal ◽  
2011 ◽  
Vol 278 (21) ◽  
pp. 4100-4111 ◽  
Author(s):  
Ai Minomo ◽  
Yu Ishima ◽  
Ulrich Kragh-Hansen ◽  
Victor T. G. Chuang ◽  
Makiyo Uchida ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Phage Display ◽  
Human Serum ◽  
Biological Characteristics ◽  
Affinity Binding ◽  
High Affinity Binding ◽  
High Affinity

Development of DNA Nanostructures for High-Affinity Binding to Human Serum Albumin

2017 ◽  
Vol 139 (21) ◽  
pp. 7355-7362 ◽  
Author(s):  
Aurélie Lacroix ◽  
Thomas G. W. Edwardson ◽  
Mark A. Hancock ◽  
Michael D. Dore ◽  
Hanadi F. Sleiman
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Affinity Binding ◽  
Dna Nanostructures ◽  
High Affinity Binding ◽  
High Affinity

scholarly journals Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin

1978 ◽  
Vol 171 (2) ◽  
pp. 453-459 ◽  
Author(s):  
C Jacobsen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Lysine Residue ◽  
Water Soluble ◽  
High Affinity ◽  
Coupling Reagent ◽  
Peptide Fraction ◽  
Short Period ◽  
High Affinity Site

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.

Optical microchips based on high-affinity recombinant protein binders—Human serum albumin detection in urine

2018 ◽  
Vol 272 ◽  
pp. 441-447 ◽  
Author(s):  
Alena Semeradtova ◽  
Marcel Stofik ◽  
Lucie Vankova ◽  
Petr Maly ◽  
Ondrej Stanek ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Recombinant Protein ◽  
Serum Albumin ◽  
Human Serum ◽  
High Affinity ◽  
Protein Binders

scholarly journals Phycocyanobilin, a bioactive tetrapyrrolic compound of blue-green alga Spirulina, binds with high affinity and competes with bilirubin for binding on human serum albumin

RSC Advances ◽  
2015 ◽  
Vol 5 (76) ◽  
pp. 61787-61798 ◽  
Author(s):  
Simeon L. Minic ◽  
Miloš Milcic ◽  
Dragana Stanic-Vucinic ◽  
Milica Radibratovic ◽  
Theodore G. Sotiroudis ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Green Alga ◽  
Blue Green Alga ◽  
Selective Binding ◽  
High Affinity

High affinity, stereo-selective binding of phycocyanobilinM-conformer to HSA, and its competition with bilirubin, warfarin and hemin for the binding to protein.

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
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