Confirmation of the mapping assignment of human serum albumin to chromosome 4 using a cloned human albumin gene

1982 ◽  
Vol 34 (4) ◽  
pp. 282-288 ◽  
Author(s):  
D.M. Kurnit ◽  
Wallner Philipp ◽  
G.A.P. Bruns
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Human Albumin ◽  
Chromosome 4 ◽  
Albumin Gene

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 A point mutation in the human serum albumin gene results in familial dysalbuminaemic hyperthyroxinaemia.

1994 ◽  
Vol 31 (5) ◽  
pp. 355-359 ◽  
Author(s):  
C E Petersen ◽  
A G Scottolini ◽  
L R Cody ◽  
M Mandel ◽  
N Reimer ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Point Mutation ◽  
Albumin Gene

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.

Genetic variants showing apparent hot-spots in the human serum albumin gene

1999 ◽  
Vol 289 (1-2) ◽  
pp. 45-55 ◽  
Author(s):  
Monica Galliano ◽  
Ulrich Kragh-Hansen ◽  
András L Tárnoky ◽  
John C Chapman ◽  
Monica Campagnoli ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Genetic Variants ◽  
Hot Spots ◽  
Albumin Gene

scholarly journals Single-center analysis of the inappropriate use of human albumin and nutritional support in hospitalized patients with hypoproteinemia in China

2021 ◽  
Vol 49 (3) ◽  
pp. 030006052098773
Author(s):  
Jin Zhang ◽  
ZheTao Zhang ◽  
TianLu Shi
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Medication Safety ◽  
Nutritional Support ◽  
Clinical Training ◽  
Human Albumin ◽  
Single Center ◽  
Rational Use ◽  
Inappropriate Use

Background This study used single-center analysis of human serum albumin clinical usage and enteral-parenteral nutritional support to establish clinical application standards for the rational use of human serum albumin. Methods A total of 1984 patients receiving human serum albumin were enrolled in this retrospective study to analyze the rational application of human serum albumin and enteral-parenteral nutritional support. Results Among 1984 patients, 1044 (52.6%) were found to have irrational applications for human serum albumin use. Major indications for irrational applications were hypoproteinemia (30.0%) and nutritional support (21.9%). Surgical departments including thoracic surgery, orthopedics, and neurosurgery had the most irrational applications, occupying 18.4%, 8.4%, and 4.2%, respectively. A total of 1627 patients (82%) required nutritional support and 745 (45.8%) had irrational nutritional support. Moreover, 694 patients (35.0%) received human serum albumin as the only source of nutritional support. Conclusions Clinical training and the establishment of an approval system should be used to enhance the rational use of human serum albumin, ensuring medication safety, reducing medical costs, and avoiding the waste of medical resources.

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 Pengaruh Pemberian Serum Albumin Manusia terhadap Kadar Albumin dalam Darah pada Anjing dengan status Hipoalbuminemia

2019 ◽  
Vol 37 (1) ◽  
pp. 34
Author(s):  
Julita Dewitri Merthayasa ◽  
Putu Devi Devi Jayanti ◽  
Soedarmanto Indarjulianto ◽  
Ryan Hadi Permana ◽  
Nadia Liswardani Destinanda ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Human Albumin ◽  
Albumin Level ◽  
Blood Levels ◽  
Total Plasma ◽  
Normal Limits ◽  
Total Plasma Protein ◽  
Before And After

Albumin consists of 50% of the total plasma protein and it is very important protein in the animal's body. Hypoalbuminemia can occurs due to various conditions, such as loss of protein nephropathy, loss of enteropathic proteins, chronic and acute diarrhea or heavy bleeding as well as malnutrition and malabsorption conditions. This study aims to determine the effect of  human serum albumin  20% infusion to increase albumin blood level in hypoalbuminemia dogs. Animals used in this study were 5 dogs whose results showed the levels of albumin below normal limits or hypoalbuminemia. Dogs with hypoalbuminemia will be infused with human serum albumin (HSA) 20% through intravenous for ± 4 hours. Then, these dogs blood will be drawn days after infusion to screen for albumin levels. The results obtained in the form of examination data of albumin blood levels in the blood before and after infusion will be analyzed with paired T-test. The results showed an increase of albumin level significantly from an average of 1.98 ± 0.356 to 2.28 ± 0.257(P <0.05). This study shows the presence of human albumin serum through intravenous infusion was able to increase albumin levels in dogs with hypoalbuminemia.

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