scholarly journals Structural changes and metal binding by proalbumins and other amino-terminal genetic variants of human serum albumin.

1987 ◽  
Vol 84 (21) ◽  
pp. 7403-7407 ◽  
Author(s):  
N. Takahashi ◽  
Y. Takahashi ◽  
F. W. Putnam
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Metal Binding ◽  
Genetic Variants ◽  
Structural Changes ◽  
Amino Terminal

Rapid detection and initial characterization of genetic variants of human serum albumin

1991 ◽  
Vol 37 (7) ◽  
pp. 1221-1224 ◽  
Author(s):  
J Merle Sheat ◽  
Robert J Peach ◽  
Peter M George
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Genetic Variants ◽  
Gel Electrophoresis ◽  
Structural Changes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl

Abstract We have studied the detection and classification of genetic variants of human serum albumin by electrophoresis. Samples from 10 patients who were heterozygous for eight different albumin variants were studied by two methods. In agarose gel electrophoresis, each of these variants has an abnormal mobility and can be classified on the basis that structural changes at the N-terminus abolish 63Ni binding. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis of whole serum, glycosylated variants are easily detected because of their greater apparent molecular mass.

The Amino-Terminal Peptide of HIV-1 gp41 Interacts with Human Serum Albumin

1993 ◽  
Vol 9 (11) ◽  
pp. 1145-1156 ◽  
Author(s):  
LARRY M. GORDON ◽  
CYRIL C. CURTAIN ◽  
VICKIE McCLOYN ◽  
ALAN KIRKPATRICK ◽  
PATRICK W. MOBLEY ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Terminal ◽  
Hiv 1

Structural Characterization of Four Genetic Variants of Human Serum Albumin Associated with Alloalbuminemia in Italy

1997 ◽  
Vol 247 (2) ◽  
pp. 476-482 ◽  
Author(s):  
Lorenzo Minchiotti ◽  
Scott Watkins ◽  
Jeanne Madison ◽  
Frank W. Putnam ◽  
Ulrich Kragh-Hansen ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structural Characterization ◽  
Genetic Variants

scholarly journals Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant.

1994 ◽  
Vol 91 (14) ◽  
pp. 6476-6480 ◽  
Author(s):  
J. Madison ◽  
M. Galliano ◽  
S. Watkins ◽  
L. Minchiotti ◽  
F. Porta ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Genetic Variants ◽  
Carboxyl Terminal

Complexation of Cm(III) with blood serum proteins: recombinant human serum albumin (rHSA)

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Nicole Adam ◽  
Cédric Y. Reitz ◽  
Anna-Lena Ditter ◽  
Petra J. Panak
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Metal Binding ◽  
Serum Proteins ◽  
Laser Fluorescence ◽  
Conditional Stability ◽  
Conditional Stability Constant ◽  
Recombinant Human Serum Albumin

Abstract The complexation of Cm(III) with the recombinant human serum albumin (rHSA) (characterized by single deletion of residue Asp-1), is studied in dependence of pH and rHSA concentration using time-resolved laser fluorescence spectroscopy (TRLFS). A Cm(III) rHSA species is formed between pH 6.4 and 10.0 with the conditional stability constant being logK = 6.47 at pH = 7.4. Competition titration experiments with Cu(II) and Zn(II) confirm complexation at the N-terminal binding site (NTS) of rHSA and exclude the involvement of the Multi-Metal Binding Site (MBS). Comparison with a previous study on Cm(III) interaction with native albumin, HSA, points out, that residue Asp-1 is involved in Cm(III) binding to HSA but is not crucial for Cm(III) complexation at the NTS. The results are of major importance for a better understanding of fundamental actinide-protein interaction mechanisms which are highly required for the identification and characterization of relevant distribution pathways of incorporated radionuclides.

scholarly journals Effect of Common Buffers and Heterocyclic Ligands on the Binding of Cu(II) at the Multimetal Binding Site in Human Serum Albumin

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Magdalena Sokołowska ◽  
Krystyna Pawlas ◽  
Wojciech Bal
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Metal Binding ◽  
Visible Range ◽  
Heterocyclic Ligands ◽  
Binding Properties ◽  
Spectral Changes ◽  
Conformational Effects

Visible-range circular dichroism titrations were used to study Cu(II) binding properties of Multimetal Binding Site (MBS) of Human Serum Albumin (HSA). The formation of ternary MBS-Cu(II)-Buffer complexes at pH 7.4 was positively verified for sodium phosphate, Tris, and Hepes, the three most common biochemical buffers. The phosphate > Hepes > Tris order of affinities, together with strong spectral changes induced specifically by Tris, indicates the presence of both Buffer-Cu(II) and Buffer-HSA interactions. All complexes are strong enough to yield a nearly 100% ternary complex formation in 0.5 mM HSA dissolved in 100 mM solutions of respective buffers. The effects of warfarin and ibuprofen, specific ligands of hydrophobic pockets I and II in HSA on the Cu(II) binding to MBS were also investigated. The effects of ibuprofen were negligible, but warfarin diminished the MBS affinity for Cu(II) by a factor of 20, as a result of indirect conformational effects. These results indicate that metal binding properties of MBS can be modulated directly and indirectly by small molecules.

Antioxidant capacity and structural changes of human serum albumin from patients in advanced stages of diabetic nephropathy and the effect of the dialysis

2015 ◽  
Vol 404 (1-2) ◽  
pp. 193-201 ◽  
Author(s):  
Marisol Rosas-Díaz ◽  
Menandro Camarillo-Cadena ◽  
Andrés Hernández-Arana ◽  
Eva Ramón-Gallegos ◽  
Rafael Medina-Navarro
Keyword(s):  
Diabetic Nephropathy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Antioxidant Capacity ◽  
Human Serum ◽  
Structural Changes ◽  
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