scholarly journals Chemical structure of two fragments of human serum albumin and their location in the albumin molecule

1975 ◽  
Vol 147 (3) ◽  
pp. 585-592 ◽  
Author(s):  
F Bellon ◽  
C Lapresle
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Chemical Structure ◽  
Human Albumin ◽  
Disulphide Bond ◽  
Alpha Chain ◽  
Disulphide Bonds ◽  
Terminal Amino ◽  
Albumin Molecule

1. ‘Inhibitor fragment’ isolated from human serum albumin degraded by rabbit cathepsin D is composed of one peptide chain with two intrachain disulphide bonds. There are two kinds of inhibitor molecules having different N-terminal amino acids: one is threonine and the other glutamine. 2. Fragment F1, isolated from inhibitor degraded by trypsin, is composed of two chains linked by a disulphide bond. There are three kinds of fragment F1. All have one alpha chain in common, which has an intrachain disulphide bond. They differ by the nature of the chain, which is linked to the alpha chain by a disulphide bond. The epsilon chain is present in trace amounts. The two other chains, beta and gamma, differ by their C-terminal amino acid, which is respectively arginine and lysine. 3. Inhibitor is composed of the last 92 or 89 residues of the human albumin molecule and fragment F1 is composed of two parts of this C-terminal portion of the albumin molecule.

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.

scholarly journals Analysis of the Binding of Aripiprazole to Human Serum Albumin: The Importance of a Chloro-Group in the Chemical Structure

ACS Omega ◽  
2018 ◽  
Vol 3 (10) ◽  
pp. 13790-13797 ◽  
Author(s):  
Keiki Sakurama ◽  
Akito Kawai ◽  
Victor Tuan Giam Chuang ◽  
Yoko Kanamori ◽  
Miyu Osa ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Chemical Structure ◽  
Chloro Group

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.

The Effects of 1-Propanol on Behaviour of Human Serum Albumin in Alkaline Solution

1993 ◽  
Vol 58 (2) ◽  
pp. 267-280
Author(s):  
Vladimír Karpenko ◽  
Rostislav Škrabana
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Transition ◽  
Point Of View ◽  
Uv Spectrophotometry ◽  
Fourth Derivative ◽  
Ph Range ◽  
Albumin Molecule

The effects of 1-propanol ant to a certain extent of ethanol on human serum albumin were studied over the pH range 7 - 13.3 and alcohol concentrations up to 20 vol.%. In some case behaviour of the native preparation was compared with albumin cleared of weaker bound fatty acids. The data obtained by UV-spectrophotometry were discussed from the point of view of individual types of chromophores as well as in a broader context of the secondary structure. The results can be summarized as follows: (a) Partial removal of bound fatty acids has an influence on the dissociation of tyrosines. (b) The effect of alcohols on this dissociation is rather complex, the permitivity of the solvent being only a part of it. (c) At high alkaline pH a series of peaks in the fourth-derivative absorption spectra appear in the region 305 - 320 nm. These peaks were shown to correspond to buried dissociated tyrosines. (d) In the presence of 1-propanol a small conformational transition of albumin molecule is observed at pH below 9.

Expression of recombinant proteins lacking methionine as N-terminal amino acid in plastids: Human serum albumin as a case study

2007 ◽  
Vol 127 (4) ◽  
pp. 593-604 ◽  
Author(s):  
Alicia Fernández-San Millán ◽  
Inmaculada Farran ◽  
Andrea Molina ◽  
Angel M. Mingo-Castel ◽  
Jon Veramendi
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Recombinant Proteins ◽  
Terminal Amino Acid ◽  
Terminal Amino

scholarly journals Physicochemical characterization of carbamylated human serum albumin: an in vitro study

RSC Advances ◽  
2019 ◽  
Vol 9 (63) ◽  
pp. 36508-36516
Author(s):  
Asim Badar ◽  
Zarina Arif ◽  
Shireen Naaz Islam ◽  
Khursheed Alam
Keyword(s):  
Amino Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Physicochemical Characterization ◽  
In Vitro Study ◽  
Terminal Amino ◽  
Carbamyl Amino Acids

Carbamylation is an ubiquitous process in which cyanate (OCN−) reacts with the N-terminal amino or ε-amino moiety and generates α-carbamyl amino acids and ε-carbamyl-lysine (homocitrulline).

scholarly journals Fungicide Tebuconazole Influences the Structure of Human Serum Albumin Molecule

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3190 ◽  
Author(s):  
Katarína Želonková ◽  
Samuel Havadej ◽  
Valéria Verebová ◽  
Beáta Holečková ◽  
Jozef Uličný ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Spectra ◽  
Spectroscopic Techniques ◽  
Binding Modes ◽  
Conformation Changes ◽  
Relevant Role ◽  
Albumin Molecule ◽  
Human Serum Albumin Molecule

Studies of interactions between pesticides and target mammalian proteins are important steps toward understanding the pesticide′s toxicity. Using calorimetric and spectroscopic methods, the interaction between triazole fungicide tebuconazole and human serum albumin has been investigated. The spectroscopic techniques showed that fluorescence quenching of human serum albumin by tebuconazole was the result of the formation of tebuconazole/human serum albumin complex with the static type as the dominant mechanism. The association constant was found to be 8.51 × 103 L/mol. The thermodynamic parameters were obtained as ΔH = −56.964 kJ/mol, ΔS = −115.98 J/mol·K. The main active interactions forming the tebuconazole/human serum albumin complex were identified as the interplay between hydrogen bonds and/or van der Waals forces, based on thermodynamic experiments. These binding modes were corroborated well by the predictions of molecular modeling. Hydrogen bonding of tebuconazole with Arg222, Ala215 and Ala291 of human serum albumin played a relevant role in binding. The conformation changes in secondary structure were characterized by circular dichroism and 3D fluorescence spectra.

scholarly journals Effect of the binding of bilirubin to either the first class or the second class of binding sites of the human serum albumin molecule on its photochemical reaction

1989 ◽  
Vol 257 (3) ◽  
pp. 711-714 ◽  
Author(s):  
S Onishi ◽  
S Itoh ◽  
K Isobe ◽  
M Ochi ◽  
T Kunikata ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Serum Bilirubin ◽  
Bilirubin Concentration ◽  
Kinetics Of ◽  
Albumin Molecule ◽  
Human Serum Albumin Molecule ◽  
Serum Bilirubin Concentration

The kinetics of the photochemical changes of bilirubin were studied at a constant concentration of bilirubin bound either to the first class or to the second class of binding sites of the human serum albumin molecule. The more the bilirubin binds to the first class of binding sites in the human serum albumin molecule, the more readily geometric photoequilibrium to give (ZE)-bilirubin takes place. The more the bilirubin binds to the second class of binding sites or allosterically transformed binding sites induced by added SDS, the more readily structural photoisomerization, i.e. the formation of (EZ)-cyclobilirubin, takes place. When the serum bilirubin concentration is at low, safe, values bilirubin binds exclusively to the first class of binding sites and serves as an antioxidant [Onishi, Yamakawa & Ogawa (1971) Perinatology 1, 373-379]; at these concentrations human serum albumin protects bilirubin from irreversible photodegradation by only allowing readily reversible geometric photoisomerization. As the serum bilirubin concentration increases to high, and potentially dangerous, values, bilirubin binds to the second class of binding sites, and under these conditions human serum albumin seems to promote the photocyclization of bilirubin. During irradiation human serum albumin seems to act by retaining low, useful, concentrations of bilirubin while facilitating irreversible photoisomerization of excess bilirubin.

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