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.

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.

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.

Synthesis of Hydroxyapatite in Microemulsion and its Adsorption Properties for Human Serum Albumin

2009 ◽  
Vol 79-82 ◽  
pp. 51-54
Author(s):  
Xian Peng Zheng ◽  
Yan Liu ◽  
Yan Ming Yang ◽  
Dong Wei ◽  
Yuan Yuan Xu ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Adsorption Capacity ◽  
Serum Protein ◽  
Ph Value ◽  
Energy Dispersive Spectrometer ◽  
High Surface ◽  
Size Analysis ◽  
Human Serum Protein

Hydroxyapatite (HAP) was synthesized in Triton X-100 microemulsion and was characterized by scanning electron microscopy (SEM), energy dispersive spectrometer (EDS). Particle size analysis results showed that the particles has nanometer size, high surface area and loose structure. The prepared HAP had high adsorption capacity to human serum protein and the adsorption of human serum protein on the surface of HAP was confirmed by SEM. The factors which influenced the adsorption capacity such as the acidity, reaction time and the concentration of adsorbent were investigated in detail and the adsorption isothermal was also obtained. The adsorption capacity reduced while the pH value increased, and the adsorption reached equilibrium when shaking time was up to 40 min. The adsorption isotherm could be fitted by the pseudo-Langmuir type. The adsorption of human serum albumin on HAP was investigated, and the influences of adsorption on the conformation of human serum albumin were studied by infrared and ultraviolet spectroscopy. It can be seen from the FT-IR spectra that the intensity of flex vibration of C=O, N-C bonds all weakened. The calculation results of ultraviolet spectrum indicated that the quantity of α spiral structure reduced from 44% to 17.12%.

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.

scholarly journals Serum proteinogram of the Campeiro horse

2019 ◽  
Vol 71 (2) ◽  
pp. 363-368
Author(s):  
A.F. Souza ◽  
J. Schade ◽  
A.F. Ramos ◽  
M.S.M. Albuquerque ◽  
G.V. Fonteque ◽  
...  
Keyword(s):  
Serum Protein ◽  
Serum Proteins ◽  
Reference Interval ◽  
Total Serum Protein ◽  
Total Serum ◽  
Serum Concentrations ◽  
Reproductive Condition ◽  
Serum Fractions ◽  
Pregnancy Status ◽  
Biuret Method

ABSTRACT The aim of this study to measure the fractions of the total serum proteins of the Campeiro horse and identify the influences of biological variants. Blood samples were taken in 138 horses of the breed Campeiro for measuring the concentration of total serum protein by the biuret method. Serum concentrations of protein fractions were measured by electrophoresis using agarose gel. Groups were formed according to age, sex and reproductive condition. The average values of serum fractions: albumin (2.85±0.36g/dl), alpha 1 (0.28±0.11g/dl), alpha 2 (0.26±0.08g/dL) beta 1 (0.57±0.15g/dl), beta 2 (0.89±0.28g/dL), gamaglobulinas (1.86±0.34g/dL), albumin/globulin ratio (0.75±0.18) and 2.5% percentile and 97.5% had slight differences in relation to the reference interval proposed for the species. They observed higher values of alpha 1 and 2 globulins in the group from that had six to eight years old and gammaglobulins in group above 13 years old. Serum protein concentrations were similar in horses and mares and between non-pregnant and pregnant. Sex and pregnancy status did not affect serum proteinogram. Alpha and gammaglobulins have higher values as the age increases. Serum proteinogram of Campeiro horses shows variations that have to be considered in the interpretation of laboratory tests.

Glycylglycylglycine as a Synthetic Standard for Serum Protein Determination

1974 ◽  
Vol 20 (1) ◽  
pp. 70-73
Author(s):  
Bernard Klein
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Bovine Serum ◽  
Molar Absorptivity ◽  
Protein Determination ◽  
Synthetic Standard ◽  
Mean Differences

Abstract Glycylglycylglycine was investigated as a reference standard for use in serum protein measurement by the biuret reaction. The tripeptide-biuret solution has a molar absorptivity of 96 at 565 nm, and absorbances at both 550 nm and 565 nm are proportional to concentration. By a manual reference procedure, the 550-nm absorbance of 1.0 g of tripeptide was equivalent to that given by 1.72 ± 0.03 g of human serum albumin or 1.43 ± 0.03 g of bovine serum albumin. By the Technicon N14b automated procedure, the absorbance of 1.0 g of tripeptide at 550 nm was equivalent to that of 1.81 ± 0.02 g of human serum albumin or 1.89 ± 0.03 g of bovine serum albumin. Results for serum protein analyses over the range 4.0 to 9.0 g/dl, when tripeptide or serum albumin was used to prepare calibration curves, showed mean differences of 0.15 g/dl in the manual mode and 0.08 g/dl in the automated mode.

Serum glycoproteins in growing pups

1962 ◽  
Vol 203 (1) ◽  
pp. 119-121 ◽  
Author(s):  
Otakar V. Sirek ◽  
Anna Sirek
Keyword(s):  
Weight Gain ◽  
Sialic Acid ◽  
Serum Protein ◽  
Total Protein ◽  
Protein Concentration ◽  
Total Serum Protein ◽  
Total Serum ◽  
Albumin Fraction ◽  
The Individual ◽  
Serum Protein Concentration

Total protein-bound hexose, hexosamine, and sialic acid were determined in sera of six littermate mongrel pups at monthly intervals from the 4th day after birth up to the age of 7 months. The concentration of the individual constituents fluctuated considerably from month to month, but the values showed neither a definite trend nor a relationship to weight gain. When the carbohydrate moiety was expressed as percentage of total serum protein concentration, the values were high in newborn pups and diminished after the 1st month of life. This was due to a rise in the concentration of total serum protein, brought about by an increase of the albumin fraction which is low in carbohydrate.

Effect of protein concentration on the determination of digoxin in serum by fluorescence polarization immunoassay.

1984 ◽  
Vol 30 (11) ◽  
pp. 1826-1829 ◽  
Author(s):  
W H Porter ◽  
V M Haver ◽  
B A Bush
Keyword(s):  
Serum Protein ◽  
Total Protein ◽  
Fluorescence Polarization ◽  
Protein Concentration ◽  
Total Serum Protein ◽  
Total Serum ◽  
Fluorescence Polarization Immunoassay ◽  
Total Protein Concentration ◽  
Protein Pellet

Abstract Determination of digoxin by fluorescence polarization immunoassay (FPIA) with the Abbott "TDx" is significantly influenced by the concentration of total serum protein. Each 10 g/L increase in serum protein results in an 8% decrease in measured digoxin. Studies with [3H]digoxin confirmed that digoxin binds to the protein pellet during the trichloroacetic acid precipitation step before the immunoassay. Serum protein, or equal concentrations of albumin or gamma-globulin, exert an equivalent effect on the apparent digoxin value. Because the total protein concentration of the assay calibrators is low (50 g/L) compared with its reference interval in serum (60-80 g/L), results by FPIA may be expected to be low by an average of 16% (range, 8-24%). Digoxin results by FPIA will be most nearly accurate when the calibrators include a total protein concentration of about 70 g/L. Patients' specimens with abnormally high or low protein content will give falsely high or low results for digoxin.

Increased serum albumin, γ globulin, immunoglobulin IgG, and IgG2 and IgG4 in autism

2002 ◽  
Vol 32 (8) ◽  
pp. 1457-1463 ◽  
Author(s):  
J. CROONENBERGHS ◽  
A. WAUTERS ◽  
K. DEVREESE ◽  
R. VERKERK ◽  
S. SCHARPE ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Serum Protein ◽  
Viral Infections ◽  
Autoimmune Disorder ◽  
Protein Electrophoresis ◽  
Serum Protein Electrophoresis ◽  
Total Serum Protein ◽  
Total Serum ◽  
Igg Subclass ◽  
Serum Concentrations

Background. Research on the biological pathophysiology of autism has found some evidence that immune alterations may play a role in the pathophysiology of that illness. As a consequence we expected to find that autism is accompanied by abnormalities in the pattern obtained in serum protein electrophoresis and in the serum immunoglobulin (Ig) and IgG subclass profile.Method. We examined whether subjects with autism showed changes in total serum protein (TSP) and the serum concentrations of albumin, α1 globulin, α2 globulin, β globulin and γ globulins, IgA, IgM and IgG and the IgG subclasses IgG1, IgG2, IgG3 and IgG4, compared with normal controls.Results. We found significantly increased concentrations of TSP in autistic subjects, which were attributable to increased serum concentrations of albumin and γ globulin. Serum IgG, IgG2 and IgG4 were also significantly raised. In autism there were significant and positive correlations between social problems and TSP and serum γ globulin and between withdrawal symptoms and TSP and serum albumin and IgG.Conclusions. The results suggest that autism is characterized by increased TSP, a unique pattern obtained in serum protein electrophoresis, i.e. increased serum albumin and IgG, and by a specific IgG subclass profile, i.e. increased serum IgG2 and IgG4. The increased serum concentrations of IgGs in autism may point towards an underlying autoimmune disorder and/or an enhanced susceptibility to infections resulting in chronic viral infections, whereas the IgG subclass skewing may reflect different cytokine-dependent influences on autoimmune B cells and their products.

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