Benzo[a]pyrene anti-diol epoxide covalently modifies human serum albumin carboxylate side chains and imidazole side chain of histidine(146)

1991 ◽  
Vol 113 (22) ◽  
pp. 8505-8509 ◽  
Author(s):  
Billy W. Day ◽  
Paul L. Skipper ◽  
Joseph Zaia ◽  
Steven R. Tannenbaum
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Side Chain ◽  
Side Chains ◽  
Diol Epoxide

Enantiospecificity of Covalent Adduct Formation by Benzo[a]pyrene anti-Diol Epoxide with Human Serum Albumin

1994 ◽  
Vol 7 (6) ◽  
pp. 829-835 ◽  
Author(s):  
Billy W. Day ◽  
Paul L. Skipper ◽  
Joseph Zaia ◽  
Kuldip Singh ◽  
Steven R. Tannenbaum
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Adduct Formation ◽  
Diol Epoxide ◽  
Covalent Adduct

Kinetic Studies of Copper(II)-exchange from L-Histidine to Human Serum Albumin and Diglycyl-L-histidine, a Peptide Mimicking the Copper(II)-transport Site of Albumin

1975 ◽  
Vol 53 (5) ◽  
pp. 710-715 ◽  
Author(s):  
Show-Jy Lau ◽  
Bibudhendra Sarkar
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Exchange Rates ◽  
Human Serum ◽  
Kinetic Studies ◽  
Side Chain ◽  
Exchange Reactions ◽  
Equilibrium Study ◽  
Rate Determining Step ◽  
The Difference

The Cu(II)-exchange reactions of L-histidine with human serum albumin and diglycyl-L-histidine were studied at pH 7.53 in 0.1 MN-ethylmorpholine–HCl buffer. The exchange rates from L-histidine to albumin and peptide were determined as 0.67 and 0.42 s−1 respectively. Those from albumin and peptide to L-histidine were obtained as 0.04 and 0.07 s−1 respectively. This result is in accord with the earlier observations of the equilibrium study that the peptide has about half the Cu(II)-binding affinity as compared to albumin. The difference in the Cu(II)-exchange rates of albumin and peptide may reflect the influence of either the COOH-terminal free carboxyl group of the peptide or the side-chain residues of the Cu(II)-binding site in the native protein or both. An exchange mechanism is proposed in which the ternary complexes are shown to play the important role in the rate-determining step in the Cu(II)-exchange between a macromolecule and a small substance.

The solvatochromic effects of side chain substitution on the binding interaction of novel tricarbocyanine dyes with human serum albumin

Talanta ◽  
2012 ◽  
Vol 92 ◽  
pp. 45-52 ◽  
Author(s):  
Garfield Beckford ◽  
Eric Owens ◽  
Maged Henary ◽  
Gabor Patonay
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Side Chain ◽  
Binding Interaction

Gradual exposure of cystine side-chain residues during urea denaturation of human serum albumin

1981 ◽  
Vol 46 (1) ◽  
pp. 48-51 ◽  
Author(s):  
Josef Chmelík ◽  
Jiří Kadleček ◽  
Vítěz Kalous
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Protein Molecule ◽  
Side Chain ◽  
Urea Denaturation ◽  
Catalytic Hydrogen ◽  
Denaturation Curve

Showing the accessibility of disulfide groups in the protein molecule, the polarographic catalytic hydrogen current (Brdicka current) was employed for the investigation of the urea denaturation of human serum albumin. The stepwise character of the denaturation curve was accounted for the gradual conformational changes of the protein molecule and related increasing accessibility of cystine side-chain residues.

scholarly journals Interaction of benzo[a]pyrene diol epoxide isomers with human serum albumin: Site specific characterisation of adducts and associated kinetics

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Hitesh V. Motwani ◽  
Emelie Westberg ◽  
Margareta Törnqvist
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Site Specific ◽  
Diol Epoxide

scholarly journals Synthesis of the native copper(II)-transport site of human serum albumin and its copper(II)-binding properties

1978 ◽  
Vol 169 (1) ◽  
pp. 61-69 ◽  
Author(s):  
K S Iyer ◽  
S J Lau ◽  
S H Laurie ◽  
B Sarkar
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Low Ph ◽  
Side Chain ◽  
Complex Species ◽  
Square Planar ◽  
Native Sequence ◽  
Ph Range ◽  
Transport Site

A derivative of the native-sequence tripeptide of the specific Cu(II)-transport site of human serum albumin, L-aspartyl-L-alanyl-L-histidine N-methylamide, was synthesized, and its binding to Cu(II) was examined to determine the influence of the side-chain groups on the Cu(II) binding. The equilibria involved in the Cu(II)-L-aspartyl-L-alanyl-L-histidine N-methylamide system were investigated by analytical potentiometry. Three complex species were found in the pH range 4-10. The same species were identified in both the visible and circular-dichroism spectra. The main species present in the physiological pH range is shown to have the same ligands around the square-planar Cu(II) ion as those reported for albumin and tripeptides diglycyl-L-histidine and its N-methylamide derivative. The results obtained from competition experiments showed that this tripeptide has a higher affinity towards Cu(II) than has albumin itself. The overall findings are compared with those from albumin. At neutral pH the side chains do not play any important role in the Cu(II) binding, but at low pH the beta-carboxyl group of the N-terminal aspartic residue becomes important. A possible competition site on albumin for Cu(II) at low pH is discussed.

Human serum albumin-benzo[a]pyrene anti-diol epoxide adduct structure elucidation by fluorescence line narrowing spectroscopy

1992 ◽  
Vol 5 (1) ◽  
pp. 71-76 ◽  
Author(s):  
Billy W. Day ◽  
Mark M. Doxtader ◽  
Robert H. Rich ◽  
Paul L. Skipper ◽  
Kuldip Singh ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Structure Elucidation ◽  
Diol Epoxide ◽  
Line Narrowing ◽  
Fluorescence Line ◽  
Fluorescence Line Narrowing

scholarly journals Synthesis of a Novel PTH1–34 Analog with Increased Human Serum Albumin Affinity

2021 ◽  
Vol 03 (01) ◽  
pp. e23-e29
Author(s):  
Si-Da Ruan ◽  
Yuan-Zhen Dong ◽  
Jian-Guang Lu ◽  
Meng-Jia Zhao ◽  
Wei-Gen Lu ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Half Life ◽  
Recombinant Protein Expression ◽  
Synthesis Process ◽  
Side Chain ◽  
Osteoporosis Therapy ◽  
Acting Agent

Parathyroid hormone (PTH)1–34 is an effective peptide drug for osteoporosis therapy. However, the half-life of PTH1–34 in vivo is short, leading to the need for frequent injections of this drug during its treatment. To prolong the half-life of PTH1–34, a novel PTH1–34 analog was generated based on fatty acid generation, and its synthesis process included recombinant protein expression, side-chain modification, and peptide decoration. The PTH1–34 variant was expressed in Escherichia coli, with a single Lys (position 27) retained as a modification site. The side chain, –AEEA-γGlu-C18 diacid, was synthesized using 2-chlorotrityl chloride resin as a solid support, and then was conjugated to the PTH1-34 variant to form PTH-Lys27-AGC. Reversed-phase chromatography confirmed a high final purity (>98%) of the target compound; in vitro bioactivity tests showed that PTH-1 receptor potency of PTH-Lys27-AGC was comparable to that of the native PTH1–34. A competitive human serum albumin binding test demonstrated a high albumin affinity of PTH-Lys27-AGC in comparison to PTH1–34. In summary, we developed a novel PTH1–34 analog, PTH-Lys27-AGC, which may be a long-acting agent for osteoporosis treatment in the future.

The Effect of Human Serum Albumin and Mercurial Diuretics on Ascites in Patients With Hepatic Cirrhosis

1950 ◽  
Vol 16 (2) ◽  
pp. 455-465 ◽  
Author(s):  
W. Paul Havens ◽  
Lewis W. Bluemle
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Hepatic Cirrhosis

II. Lokalisation der Placenta mit 113Inm- Human-Serum-Albumin

1969 ◽  
Vol 08 (01) ◽  
pp. 15-21 ◽  
Author(s):  
K. E. Scheer ◽  
J. Heep ◽  
W. Maier-Borst ◽  
W. J. Lorenz ◽  
H. Sinn ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Vena Cava ◽  
Placenta Praevia ◽  
Wird Eine

ZusammenfassungNach tierexperimentellen Voruntersuchungen wurde die Placentographie mit trägerfreiem 113Inm -HSA als klinische Methode eingeführt. Vor Amniocentesen und bei Verdacht auf Placenta praevia werden Placentographien geschrieben. Den Schwangeren wird eine Aktivität von 500 μCi in die Cubitalvene injiziert. Die der Aktivität entsprechende Indiummenge ist kleiner als 0,1 ng. Die fetale Strahlenbelastung liegt unter lOmrad. Bei Anwendung von 113Inm-HSA entfällt eine Blockade der mütterlichen und fetalen Schilddrüsen. Die genaue Abgrenzung einer Placenta praevia wird nicht durch eine Blasenaktivität beeinträchtigt.Es wurden bisher 19 Placentalokalisationen durchgeführt. In allen Fällen konnte der Placentasitz eindeutig festgestellt werden. Bedingt durch die lange Liegezeit beim Aufnehmen eines Szintigramms kam es in zwei Fällen zu einem Vena-Cava-Kompressions-Syndrom. Zur Verhinderung dieser klinischen Zwischenfälle werden inzwischen Placentographien mit der Anger-Kamera aufgenommen. Mit Hilfe des divergierenden Kollimators konnte der gesamte Abdominalbereich erfaßt werden. Die Aufnahmezeit konnte auf 7 — 10 Minuten verkürzt werden. Die intravenöse injizierte Aktivität betrug bei dieser Methode ebenfalls 500 μCi. Der diagnostische Aussagewert der Kamerabilder ist szintigraphischen Aufnahmen gleichwertig.

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