scholarly journals Studies in Bisalbuminemia: Binding Properties of the Two Albumins

Blood ◽  
1962 ◽  
Vol 20 (2) ◽  
pp. 156-164 ◽  
Author(s):  
EDWARD J. SARCIONE ◽  
C. WILLIAM AUNGST
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Total Serum ◽  
Binding Properties ◽  
Normal Human ◽  
Serum Components

Abstract 1. An abnormal serum protein pattern in a patient with Wegener’s granulomatosis and five of his relatives was identified as bisalbuminemia by electrophoretic and immunochemical methods. 2. With the exception of the patient with Wegener’s syndrome, the presence of bisalbuminemia was not associated with a significant change in total serum proteins, total albumin, serum components other than albumin, or any disease. 3. Addition of I131-thyroxine to bisalbumin sera resulted in thyroxine binding by albumin B but not by albumin A. The failure of albumin A to bind added I131-thyroxine leads to speculation that, in this family, neither albumin A nor B are identical to normal human serum albumin.

Standards for Total Serum Protein Assays— A Collaborative Study

1975 ◽  
Vol 21 (8) ◽  
pp. 1159-1166 ◽  
Author(s):  
Basil T Doumas
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Bovine Serum ◽  
Total Serum Protein ◽  
Total Serum ◽  
Final Reaction ◽  
Protein Assays

Abstract We have studied the standardization of total serum protein assay with the biuret reaction. Standard solutions were prepared from lyophilized preparations of human serum albumin and bovine serum albumin, with corrections made for volatile material and ash contents. These solutions and a solution of crystalline albumin standard were analyzed with a new stable biuret reagent, to establish absorptivity values (values for the absorbance of a 1 g/liter final reaction mixture). The mean values obtained were 0.302, 0.292, and 0.290 for human serum albumin, bovine serum albumin, and the crystalline albumin, respectively. We believe that the established absorptivity value will improve the accuracy of serum protein determinations. We studied the linearity of the relation between color produced and protein concentration, with use of the solutions described above and a serum pool. The color adheres to Beer's law up to the highest concentration tested: 3 g/liter for HSA and BSA, and 2.8 g/liter for serum in the final reaction mixture. The new biuret reagent has been stable for one year at room temperature. We recommend the use of bovine serum albumin as a primary standard for serum protein assays. It is inexpensive, easily available, and exhibits the best linearity in the biuret reaction.

Three turbidimetric methods for determining total protein compared.

1985 ◽  
Vol 31 (8) ◽  
pp. 1377-1380 ◽  
Author(s):  
H H Nishi ◽  
R J Elin
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Protein Concentration ◽  
Total Serum Protein ◽  
Total Serum ◽  
Benzethonium Chloride ◽  
Human Serum Protein ◽  
Biuret Method

Abstract We used human serum protein fractions to evaluate the sensitivity and bias of three turbidimetric methods for determining concentrations of proteins. Each fraction (Cohn Fractions II, III, IV, and V) was assigned a protein concentration value that was determined by the biuret method, which we calibrated with purified monomer of human serum albumin. All three turbidimetric methods (those involving sulfosalicylic acid/sodium sulfate, trichloroacetic acid, and alkaline benzethonium chloride) gave acceptable results for Fraction V with crystallized human serum albumin as the reference material, but there was bias by each of the three methods for the three globulin fractions. The method involving alkaline benzethonium chloride with measurement at 450 nm had the best sensitivity within the range of linearity and the most consistent bias among the three globulin fractions. These results define the dilemma for valid calibration of these methods for total serum protein in cerebrospinal fluid and urine.

Cigarette smoke induces alterations in the drug-binding properties of human serum albumin

2014 ◽  
Vol 52 (4) ◽  
pp. 166-174 ◽  
Author(s):  
Marco Clerici ◽  
Graziano Colombo ◽  
Francesco Secundo ◽  
Nicoletta Gagliano ◽  
Roberto Colombo ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cigarette Smoke ◽  
Drug Binding ◽  
Binding Properties

scholarly journals Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

RSC Advances ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 4742-4749 ◽  
Author(s):  
Zili Suo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
Peixiao Tang ◽  
Ruixue Gan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Simulations ◽  
Binding Properties

Probing the binding properties of trametinib to human serum albumin.

THE ETIOLOGY OF HYPOPROTEINEMIA IN A PATIENT WITH CONGENITAL CHYLOUS ASCITES

PEDIATRICS ◽  
1962 ◽  
Vol 30 (5) ◽  
pp. 696-706
Author(s):  
Fred S. Rosen ◽  
David H. Smith ◽  
Ralph Earle ◽  
Charles A. Janeway ◽  
David Gitlin
Keyword(s):  
Gastrointestinal Tract ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Chylous Ascites ◽  
Lower Extremities ◽  
Characteristic Finding

An infant with congenital chylous ascites and Milroy's disease, as well as two patients with Milroy's disease of the lower extremities, have been studied with regard to the turnover of I131-labeled human serum albumin. The children with Milroy's diease had a normal turnover of radioiodinted albumin, whereas the child with congenital chylous ascites had a markedly increased turnover due to loss of serum protein into the gastrointestinal tract. The hypoproteinemia which is a characteristic finding in congenital chylous ascites may be due to such gastrointestinal loss of protein in serum.

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.

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