scholarly journals Large fragments of human serum albumin

1977 ◽  
Vol 161 (3) ◽  
pp. 619-625 ◽  
Author(s):  
M J Geisow ◽  
G H Beaven
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Tertiary Structure ◽  
Human Albumin ◽  
Low Ph ◽  
Bovine Albumin ◽  
Linkage Pattern ◽  
Peptic Digestion ◽  
Similar Tertiary Structure

Large fragments of human serum albumin were produced by treatment of the native protein with pepsin at pH3.5. Published sequences of human albumin [Behrens, Spiekerman & Brown (1975) Fed. Proc. Fed. Am. Soc. Exp. Biol. 34, 591; Meloun, Moravek & Kostka (1975) FEBSLett.58, 134-137]were used to locate the fragments in the primary structure. The fragments support both the sequence and proposed disulphide-linkage pattern (Behrens et al., 1975). As the pH of a solution of albumin is lowered from pH4 to pH3.5, the protein undergoes a reversible conformational change known as the N-F transition. The distribution of large fragments of human albumin digested with pepsin in the above pH region was critically dependent on pH. It appeared that this distribution was dependent on the conformation of the protein at low pH, rather than the activity of pepsin. The yields of the large fragments produced by peptic digestion at different values of pH suggested that the C-terminal region of albumin unfolds or separates from the rest of the molecule during the N-F transition. The similarity of peptic fragments of human and bovine albumin produced under identical conditions supports the proposed similar tertiary structure of these molecules.

scholarly journals A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part II

2021 ◽  
Vol 89 (3) ◽  
pp. 30
Author(s):  
Anna Ploch-Jankowska ◽  
Danuta Pentak ◽  
Jacek E. Nycz
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Tertiary Structure ◽  
Temperature Characteristic ◽  
The Body ◽  
Structural Modifications ◽  
Influence Of Temperature On ◽  
Exogenous Substances

Human serum albumin (HSA) is the most abundant human plasma protein. HSA plays a crucial role in many binding endos- and exogenous substances, which affects their pharmacological effect. The innovative aspect of the study is not only the interaction of fatted (HSA) and defatted (dHSA) human serum albumin with ibuprofen (IBU), but the analysis of the influence of temperature on the structural modifications of albumin and the interaction between the drug and proteins from the temperature characteristic of near hypothermia (308 K) to the temperature reflecting inflammation in the body (312 K and 314 K). Ibuprofen is a non-steroidal anti-inflammatory drug. IBU is used to relieve acute pain, inflammation, and fever. To determine ibuprofen’s binding site in the tertiary structure of HSA and dHSA, fluorescence spectroscopy was used. On its basis, the fluorescent emissive spectra of albumin (5 × 10−6 mol/dm3) without and with the presence of ibuprofen (1 × 10−5–1 × 10−4 mol/dm3) was recorded. The IBU-HSA complex’s fluorescence was excited by radiation of wavelengths of λex 275 nm and λex 295 nm. Spectrophotometric spectroscopy allowed for recording the absorbance spectra (zero-order and second derivative absorption spectra) of HSA and dHSA under the influence of ibuprofen (1 × 10−4 mol/dm3). To characterize the changes of albumin structure the presence of IBU, circular dichroism was used. The data obtained show that the presence of fatty acids and human serum albumin temperature influences the strength and type of interaction between serum albumin and drug. Ibuprofen binds more strongly to defatted human serum albumin than to albumin in the presence of fatty acids. Additionally, stronger complexes are formed with increasing temperatures. The competitive binding of ibuprofen and fatty acids to albumin may influence the concentration of free drug fraction and thus its therapeutic effect.

scholarly journals Partial non-cleavage by cyanogen bromide of a methionine–cystine bond from human serum albumin and bovine α-lactalbumin

1979 ◽  
Vol 177 (1) ◽  
pp. 251-254 ◽  
Author(s):  
N Doyen ◽  
C Lapresle
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cyanogen Bromide ◽  
Human Albumin ◽  
Alpha Lactalbumin

When human albumin was treated with CNBr, a fragment designated D was obtained and attributed to the absence from some of the albumin molecules of methionine at position 123 [Lapresle & Doyen (1975) Biochem. J. 151, 637-643]. The present study shows that methionine-123 is converted into homoserine without cleavage of the subsequent methionine-cystine bond. With bovine alpha-lactalbumin, a further example of non-cleavage of a methionine-cystine bond with conversion of methionine into homoserine is reported.

Ausscheidung von 131J-Humanalbumin im Primärharn der Froschniere

1959 ◽  
Vol 14 (5) ◽  
pp. 323-327 ◽  
Author(s):  
Werner Heinzel ◽  
Ekkehard Kallee
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Proteins ◽  
Human Albumin ◽  
Protein Solution ◽  
Bladder Urine

1. The glomerular capsules of 8 Bombinata toads have been tapped. The glomerula have been found to excrete 0.035-0.15 μg of protein in about 0.11 μl of urine per hour, i. e., a 0.1 p.c. protein solution.2. Radioiodinated human serum albumin when injected intraperitoneally was excreted by the toad glomerula into the primary urine and resorbed back by the tubuli in principle in the same ways as toad serum proteins. However, the human albumin was excreted by the glomerula to a significantly larger extent than toad proteins.3. The concentration of both toad protein and 131I-labelled human albumin was approximately seven times lower in the bladder urine than in the primary urine.

scholarly journals Molten globule-like state of human serum albumin at low pH

1999 ◽  
Vol 266 (1) ◽  
pp. 26-32 ◽  
Author(s):  
Salman Muzammil ◽  
Yogesh Kumar ◽  
Saad Tayyab
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molten Globule ◽  
Low Ph

At very low concentrations known chaotropes act as kosmotropes for the N and B isoforms of human serum albumin

2013 ◽  
Vol 91 (2) ◽  
pp. 72-78 ◽  
Author(s):  
Priyankar Sen ◽  
Mohd Moin Khan ◽  
Asif Equbal ◽  
Ejaz Ahmad ◽  
Rizwan Hasan Khan
Keyword(s):  
Protein Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interaction ◽  
Tertiary Structure ◽  
Guanidine Hydrochloride ◽  
Micelle Formation ◽  
Low Concentrations ◽  
Secondary And Tertiary Structure

Very few studies have been done to understand the effect of millimolar concentrations of chaotropes on protein structure. In our previous study we observed that the secondary and tertiary structure of human serum albumin (HSA) increases in the presence of 5 mmol/L urea. Micelle formation in amphoteric detergents increases in the presence of equivalent concentrations of urea. Here, we observed a significant increase in the secondary and tertiary structure of HSA. Interestingly, guanidine hydrochloride, another chaotropic agent, also shows a similar effect. Our results show electrostatic interaction may play a role in neutral to basic transition in HSA. This study further supports the claim that at millimolar concentrations the chaotropes may act as kosmotropes for proteins.

DENATURATION OF HUMAN SERUM ALBUMIN BY CERIUM (III) CHLORIDE

2013 ◽  
Vol 08 (01n02) ◽  
pp. 59-71
Author(s):  
G. REZAEI BEHBAHANI ◽  
M. SHALBAFAN ◽  
N. GHEIBI ◽  
L. BARZEGAR ◽  
H. REZAEI BEHBAHANI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Tertiary Structure ◽  
Fluorescence Emission ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Spectroscopic Methods ◽  
Irreversible Denaturation

Cerium (III) Chloride-induced conformational changes of human serum albumin, HSA, in phosphate buffer, 10 mM at pH 7.4 was investigated, using isothermal titration calorimetry (ITC), UV and fluorescence emission spectroscopic methods. The results indicate that CeCl3, Ce3+, induces irreversible denaturation of the HSA structure. The UV absorption intensity of HSA + Ce3+ shows a slight blueshift in the absorbance wavelength with increasing Ce3+ concentration. The fluorescence intensity was increased regularly and a slight redshift was observed in the emission wavelength. The HSA + Ce3+ complex quenches the fluorescence of HSA and changes the microenvironment of tryptophan residue. The emission intensity increases suggesting the loss of the tertiary structure of HSA. The results obtained from the ITC data are in agreement with the spectroscopic methods. The strong negative cooperativity of Ce3+ binding with HSA (Table 1) recovered from the extended solvation model, indicates that HSA has been denatured as a result of its interaction with Ce3+ ions.

Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

2016 ◽  
Vol 153 ◽  
pp. 560-565 ◽  
Author(s):  
A. Szkudlarek ◽  
M. Maciążek-Jurczyk ◽  
M. Chudzik ◽  
J. Równicka-Zubik ◽  
A. Sułkowska
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Spectroscopic Study ◽  
Human Serum ◽  
Tertiary Structure

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.

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