The Disulfide Bonds of Human Serum Albumin and Bovine γ-Globulin1

1957 ◽  
Vol 79 (1) ◽  
pp. 134-139 ◽  
Author(s):  
Gabor Markus ◽  
Fred Karush
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds

Microheterogeneity of human serum albumin: evidence for differences in reducibility of disulfide linkages

1968 ◽  
Vol 46 (8) ◽  
pp. 789-795 ◽  
Author(s):  
A. F. S. A. Habeeb
Keyword(s):  
Human Serum Albumin ◽  
Sodium Dodecyl Sulfate ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Free Amino ◽  
Sodium Dodecyl ◽  
Amino Groups ◽  
Trinitrobenzenesulfonic Acid ◽  
Disulfide Linkages

Studies were designed to determine the causes of the microheterogeneity of human serum albumin. Human serum albumin in 3 M KCl was fractionated in a stepwise manner by lowering the pH. The resultant fractions showed similarities in: (a) the reactivity of ε-amino groups with trinitrobenzenesulfonic acid, (b) the binding of sodium dodecyl sulfate to the free amino groups, and (c) the ability to precipitate with anti-human serum albumin. Conversely, differences existed in the susceptibility to reduction of disulfide bonds of the various fractions with β-mercaptoethanol, which suggested that the microheterogeneity of human serum albumin and its fraction may be due, in part at least, to differences in the pairing of the disulfide bonds.

Mechanism of denaturation of human serum albumin by urea

1988 ◽  
Vol 53 (2) ◽  
pp. 411-422 ◽  
Author(s):  
Josef Chmelík ◽  
Pavel Anzenbacher ◽  
Jitka Chmelíková ◽  
Milada Matějčková ◽  
Vítěz Kalous
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Polyacrylamide Gel Electrophoresis ◽  
Helical Structure ◽  
Random Coil ◽  
Gel Chromatography ◽  
Uv Spectrophotometry ◽  
Comparison Of The Results

The mechanism of denaturation of human serum albumin by urea was examined by polarography, polarimetry, circular dichroism, UV-spectrophotometry, gel chromatography, and polyacrylamide gel electrophoresis. Comparison of the results obtained by these methods shows that this reaction is a complex process which cannot be described by a two-state denaturation model. It has been demonstrated that the different states which denaturation produces arise under different denaturation conditions. The different behavior of various species of human serum albumin (monomer, mercaptalbumin and nonmercaptalbumin) during denaturation by urea was examined. As a result the following probable denaturation scheme was proposed: The denaturation of human serum albumin by urea is regarded as a stepwise process involving one stable intermediary product at least ( demonstrated electrophoretically). After the rapid initial change of the ordered helical structure extensive hydrophobic domains of the molecule remain folded. Cystine residues are gradually liberated from these domains. Denaturated mercaptalbumin has the conformation of a random coil in which the pairing of native disulfide bonds has been altered because of SH-S-S interchange reactions; in contrast native disulfide bonds are retained in nonmercaptalbumin.

Different rates of formation of secondary and tertiary structure during renaturation of urea-denatured human serum albumin

1989 ◽  
Vol 54 (9) ◽  
pp. 2542-2549 ◽  
Author(s):  
Josef Chmelík
Keyword(s):  
Protein Folding ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Tertiary Structure ◽  
Hydrophobic Interactions ◽  
Protein Structures ◽  
Three Dimensional ◽  
Comparison Of The Results

A comparison of the results of our polarimetric measurements with the polarographic experiments reported earlier shows that the restoration of the secondary structure during the renaturation of human serum albumin is a process which is faster than the formation of the tertiary structure. These results, which are in agreement with the data on the kinetic control of protein folding, are discussed from the viewpoint of the importance of the individual types of interactions which take place during the formation and stabilization of three-dimensional protein structures. We have been able to demonstrate the great importance of electrostatic and hydrophobic interactions which together with the disulfide bonds are essential for the reversibility of the denaturation phenomena. The discussion also shows the essential role which evolution processes play in the selection of the mode of protein folding.

Paclitaxel loaded human serum albumin nanoparticles stabilized with intermolecular disulfide bonds

MedChemComm ◽  
2014 ◽  
Vol 5 (11) ◽  
pp. 1658-1663 ◽  
Author(s):  
Shufang Zhao ◽  
Wentan Wang ◽  
Yanbin Huang ◽  
Yuhang Fu ◽  
Yi Cheng
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Thiol Groups ◽  
Cross Link ◽  
Albumin Nanoparticles ◽  
Intermolecular Disulfide Bonds ◽  
Protein Disulfide

A self-cross-link strategy was adopted to form inter-protein disulfide crosslinks with albumin's own thiol groups. PTX was further entrapped non-covalently in the HSA matrix to form paclitaxel loaded HSA nanoparticles (PTX-HSA-NPs).

Human serum albumin (HSA) nanoparticles stabilized with intermolecular disulfide bonds

2013 ◽  
Vol 49 (22) ◽  
pp. 2234 ◽  
Author(s):  
Wentan Wang ◽  
Yanbin Huang ◽  
Shufang Zhao ◽  
Ting Shao ◽  
Yi Cheng
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Intermolecular Disulfide Bonds

Disulfide bonds in human serum albumin

1977 ◽  
Vol 42 (2) ◽  
pp. 564-579 ◽  
Author(s):  
M. A. Saber ◽  
P. Stöckbauer ◽  
L. Morávek ◽  
B. Meloun
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds

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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