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.

Chromatographic profiles of cyanogen bromide fragments of unreduced human serum albumin on immobilized Cibacron Blue F3G-A

1993 ◽  
Vol 639 (2) ◽  
pp. 341-345 ◽  
Author(s):  
Anna Compagnini ◽  
Maria Fichera ◽  
Salvatore Fisichella ◽  
Salvatore Foti ◽  
Rosaria Saletti
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cyanogen Bromide ◽  
Cibacron Blue ◽  
Chromatographic Profiles

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.

Steric accessibility of tyrosine residues in human serum albumin

1979 ◽  
Vol 44 (5) ◽  
pp. 1657-1670 ◽  
Author(s):  
Ladislav Morávek ◽  
Mohamed Ali Saber ◽  
Bedřich Meloun
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Amino Acid Analysis ◽  
Cyanogen Bromide ◽  
Tyrosine Residues ◽  
Steric Accessibility ◽  
The Individual

Human serum albumin was nitrated by an excess of tetranitromethane at pH 8.0. As shown by amino acid analysis, of the 18 tyrosine residues present in albumin about 7-7.5 residues remain unaltered, 9 residues are converted into 3-nitrotyrosine, and 1.2 residue into 3,5-dinitrotyrosine. The nitrated albumin was digested with cyanogen bromide to three fragments which comprise the whole original molecule. The individual fragments were converted into their S-sulfo derivatives and the latter digested with chymotrypsin or stepwise with trypsin and thermolysin. The yellow, nitrotyrosine-containing peptides were isolated from the digest and the positions of nitrated tyrosine residues in albumin thus located. Residues No 30, 148, 150, 161, 334, 341, 401, and 411 were identified as strongly nitrated and residues No 84, 138, 452, and 497 as medium nitrated. Residues No 140, 263, 319, 332, 353, and 367 either react weakly or were not found in nitrated form. Residue No 411 and partly also 161 were converted into 3,5-dinitrotyrosine. The accessibility of the individual tyrosine residues to the nitrating agent is discussed with respect to their positions in disulfide loops and hypothetic parts of the secondary structure of albumin.

scholarly journals Binding and Relaxometric Properties of Heme Complexes with Cyanogen Bromide Fragments of Human Serum Albumin

2002 ◽  
Vol 83 (4) ◽  
pp. 2248-2258 ◽  
Author(s):  
Enrico Monzani ◽  
Maria Curto ◽  
Monica Galliano ◽  
Lorenzo Minchiotti ◽  
Silvio Aime ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cyanogen Bromide

scholarly journals Cyanogen Bromide Fragments of Human Serum Albumin

1971 ◽  
Vol 246 (15) ◽  
pp. 4744-4750 ◽  
Author(s):  
Rapier H. McMenamy ◽  
Howard M. Dintzis ◽  
Frank Watson
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cyanogen Bromide

scholarly journals Influence of Piracetam on Gliclazide—Glycated Human Serum Albumin Interaction. A Spectrofluorometric Study

Molecules ◽  
2018 ◽  
Vol 24 (1) ◽  
pp. 111 ◽  
Author(s):  
Agnieszka Szkudlarek ◽  
Jadwiga Pożycka ◽  
Małgorzata Maciążek-Jurczyk
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Glycated Albumin ◽  
Human Albumin ◽  
Protein Glycation ◽  
Monitoring Therapy ◽  
Glycation End Products ◽  
Local Accumulation

Advanced Glycation End-Products (AGEs) are created in the last step of protein glycation and can be a factor in aging and in the development or worsening of many degenerative diseases (diabetes, chronic kidney disease, atherosclerosis, Alzheimer’s disease, etc.). Albumin is the most susceptible to glycation plasma protein. Modified albumin by AGEs may be more resistant to enzymatic degradation, which further increases the local accumulation of AGEs in tissues. The aim of the present study was to analyze in vitro glycation of serum albumin in the presence of piracetam (PIR) and the gliclazide (GLZ)-glycated albumin interaction. The analysis of PIR as an inhibitor and GLZ interaction with nonglycated human albumin (HSA) and glycated by fructose human albumin (gHSAFRC), in the absence and presence of piracetam (gHSAFRC-PIR), was performed by fluorescence quenching of macromolecules. On the basis of obtained data we concluded that under the influence of glycation, association constant ( K a ) of gliclazide to human serum albumin decreases and GLZ binds to HSA with less strength than under physiological conditions. PIR strongly inhibited the formation of AGEs in the system where the efficiency of HSA glycation was the largest. The analysis of piracetam influence on the GLZ-glycated albumin interaction has shown that piracetam increases the binding strength of GLZ to glycated albumin and weakens its therapeutic effect. Based on the obtained data we concluded that monitoring therapy and precautions are required in the treatment when the combinations of gliclazide and piracetam are used at the same time.

Sign in / Sign up

Export Citation Format

Share Document