An Improved Method for Determination of Serum Albumin and Globulin

1966 ◽  
Vol 12 (4) ◽  
pp. 194-205 ◽  
Author(s):  
Alberto Fernandez ◽  
Charles Sobel ◽  
Harry Goldenberg
Keyword(s):  
Serum Albumin ◽  
Sodium Acetate ◽  
Reliable Method ◽  
Serum Proteins ◽  
Globulin Fraction ◽  
Supernatant Fluid ◽  
Improved Method ◽  
Albumin Fraction

Abstract A simple and reliable method has been developed for the analysis of serum proteins. Globulins are precipitated from serum with HCI- ethanol. The albumin remains in the supernatant fluid. The albumin fraction is then precipitated by alcoholic sodium acetate. The proteins are redissolved and determined colorimetrically following their reaction with the biuret reagent. Recovery and electrophoretic studies indicate that the method affords a clean-cut separation of albumin from the globulin fraction. Lipemia does not appear to interfere with the analysis.

OBSERVATIONS ON THE PHYSIOLOGICAL HALF-LIFE OF SERUM PROTEINS IN THE COCKEREL AND THE LAYING PULLET

1957 ◽  
Vol 35 (5) ◽  
pp. 281-291 ◽  
Author(s):  
W. E. Vanstone ◽  
W. F. Oliver ◽  
W. A. Maw ◽  
R. H. Common
Keyword(s):  
Oral Administration ◽  
Serum Albumin ◽  
Half Life ◽  
Initial Phase ◽  
Serum Proteins ◽  
Specific Activity ◽  
Yolk Protein ◽  
Globulin Fraction ◽  
Serum Globulin

The serum proteins of two cockerels and two pullets were labelled by oral administration of S35-L-methionine. The subsequent decline of specific activity of serum proteins indicated physiological half-lives of approximately 6.5 days for both serum albumin and serum globulin in the cockerels. One pullet continued in active lay and the half-life of its serum albumin was approximately 8.5 days; the decline of specific activity of the globulin fraction displayed a relatively steep initial phase; the succeeding decline gave a half-life of approximately 4.6 days; the half-life of the serum phosphoprotein fraction was probably considerably less. These results are discussed in terms of estimated replacement rates of the proteins. The second pullet stopped laying and the results with this bird are discussed separately. The average specific activity of yolk protein attained a maximum in the egg laid on the 6th day after labelling. The subsequent decline in average specific activity of yolk protein with time followed a logarithmic course.

scholarly journals Erratum

1966 ◽  
Vol 12 (6) ◽  
pp. 368-368
Keyword(s):  
Serum Albumin ◽  
Improved Method ◽  
First Line

Abstract The paper "An Improved Method for Determination of Serum Albumin and Globulin" by Alberto Fernandez, Charles Sobel, and Harry Goldenberg in the April issue of the Journal, contained an error. On page 195, underReagents, the first line should read: NaCl, 0.85% (w/v)

scholarly journals Efficacy of protein hydrolysate in the restoration of serum protein in hyperimmunized horses after blood depletion

1947 ◽  
Vol 45 (1) ◽  
pp. 56-58
Author(s):  
P. N. Basu ◽  
Sudhindra Nath Sen
Keyword(s):  
Serum Albumin ◽  
Protein Content ◽  
Serum Protein ◽  
Protein Hydrolysate ◽  
Globulin Fraction ◽  
Serum Globulin ◽  
Albumin Fraction

1. Treatment with enzymic hydrolysate of protein after blood depletion has a significant action in restoring serum protein content.2. Blood depletion of hyperimmunized horses alters the serum globulin fraction much more markedly than the serum albumin fraction.Our thanks are due to Dr R. N. Roy and Mr Diptish Chakraborty for useful help.

Electrophoretic Migration Pattern of Serum Glutamic Oxalacetic Transaminase

1958 ◽  
Vol 4 (1) ◽  
pp. 13-21 ◽  
Author(s):  
Herndon G Shepherd ◽  
Hugh J McDonald
Keyword(s):  
Pyridoxal Phosphate ◽  
Serum Proteins ◽  
Migration Pattern ◽  
Globulin Fraction ◽  
Transaminase Activity ◽  
Rat Serum ◽  
Glutamic Oxalacetic Transaminase ◽  
Electrophoretic Migration ◽  
Serum Glutamic Oxalacetic Transaminase

Abstract Using the combined technics of the ionographic separation of serum proteins in a paper-stabilized medium, as described by McDonald et al. (16, 17, 18), and the spectrophotometric procedure for the determination of transaminase activity developed by Karmen (3, 14), the electrophoretic migration pattern of the enzyme glutamic oxalacetic transaminase in rat serum has been examined. The major portion of the transaminase activity has been found to be associated with the α-2 globulin fraction of the serum proteins. Further evidence has been presented for the assumption of a nonionic linkage between the enzyme and its coenzyme, pyridoxal phosphate.

OBSERVATIONS ON THE PHYSIOLOGICAL HALF-LIFE OF SERUM PROTEINS IN THE COCKEREL AND THE LAYING PULLET

1957 ◽  
Vol 35 (1) ◽  
pp. 281-291 ◽  
Author(s):  
W. E. Vanstone ◽  
W. F. Oliver ◽  
W. A. Maw ◽  
R. H. Common
Keyword(s):  
Oral Administration ◽  
Serum Albumin ◽  
Half Life ◽  
Initial Phase ◽  
Serum Proteins ◽  
Specific Activity ◽  
Yolk Protein ◽  
Globulin Fraction ◽  
Serum Globulin

The serum proteins of two cockerels and two pullets were labelled by oral administration of S35-L-methionine. The subsequent decline of specific activity of serum proteins indicated physiological half-lives of approximately 6.5 days for both serum albumin and serum globulin in the cockerels. One pullet continued in active lay and the half-life of its serum albumin was approximately 8.5 days; the decline of specific activity of the globulin fraction displayed a relatively steep initial phase; the succeeding decline gave a half-life of approximately 4.6 days; the half-life of the serum phosphoprotein fraction was probably considerably less. These results are discussed in terms of estimated replacement rates of the proteins. The second pullet stopped laying and the results with this bird are discussed separately. The average specific activity of yolk protein attained a maximum in the egg laid on the 6th day after labelling. The subsequent decline in average specific activity of yolk protein with time followed a logarithmic course.

SERUM TRIIODOTHYRONINE DETERMINATION BY SATURATION ANALYSIS

1973 ◽  
Vol 72 (4) ◽  
pp. 714-726 ◽  
Author(s):  
A. Burger ◽  
B. Miller ◽  
C. Sakoloff ◽  
M. B. Vallotton
Keyword(s):  
Ionic Strength ◽  
Limit Of Detection ◽  
Improved Method ◽  
Accuracy Of Measurement ◽  
Tracer Amount ◽  
The Mean ◽  
Physiological Values ◽  
Hyperthyroid Patients ◽  
Solvent Blank

ABSTRACT An improved method for the determination of serum triiodothyronine (T3) has been developed. After addition of a tracer amount of the hormone, T3 was extracted from 1 ml serum under conditions of pH and ionic strength which favoured T3 extraction (89%) over thyroxine (T4) extraction (58%). Chromatography of the extracted material on Sephadex LH-20 separated T3 completely from residual T4. The T3 eluate was dried, then re-dissolved in 0.5 ml NaOH 0.04 n. To 0.2 ml duplicate aliquots, a standard amount of TBG was added for the competitive protein analysis. After one hour incubation at 4°C, separation of bound from free T3 was achieved on small Sephadex G-25 columns. Overall recovery was 67 ± 10.8% and correction for the loss was made. The solvent blank was 37 ± 27 (sd) ng/100 ml. Accuracy of measurement of known quantities of T3 added to serum was 98.4%. The coefficient of variation within the assay was 6.2% and between the assays it was 11.4%. The limit of detection (0.1 ng) corresponded to a concentration of 25 ng/100 ml. T4 added to serum did not interfere with T3 determination until high non-physiological values were reached. The mean ± sd serum T3 in 54 euthyroid subjects was 153 ± 58 ng/100 ml and in 24 hyperthyroid patients it was 428 ±186 ng/100 ml; 4 out of the 24 hyperthyroid values were within 2 sd of the mean euthyroid group. All the values found in the euthyroid group were well above the limit of detection of the method.

An Improved Method for the Determination of Metabolic Fecal P

1957 ◽  
Vol 16 (1) ◽  
pp. 201-206 ◽  
Author(s):  
J. R. Luick ◽  
G. P. Lofgreen
Keyword(s):  
Improved Method
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