scholarly journals Determination of Bilirubin with Precipitation of the Plasma Proteins

1950 ◽  
Vol 3 (3) ◽  
pp. 248-259 ◽  
Author(s):  
E. J. King ◽  
R. V. Coxon
Keyword(s):  
Plasma Proteins

scholarly journals Evaluation of free and total L-thyroxine in serum by a commercial procedure.

1981 ◽  
Vol 27 (1) ◽  
pp. 149-152 ◽  
Author(s):  
M J Obregon ◽  
A Kurtz ◽  
R Ekins ◽  
G Morreale de Escobar
Keyword(s):  
Pregnant Women ◽  
Plasma Proteins ◽  
Diagnostic Value ◽  
Free Thyroxine ◽  
Total Thyroxine ◽  
Dialysis Method ◽  
Hypothyroid Patients ◽  
Hyperthyroid Patients ◽  
Normal Controls

Abstract We assessed a commercial kit (Corning Medical) for "free" and total thyroxine determination, results being compared to those obtained by the Ekins and Ellis dialysis method (free thyroxine) and the method of Weeke and Orskov (total thyroxine). The kit procedure permits determination of both free and total thyroxine within 4 to 5 h, and the combined results may disclose changes in binding to plasma proteins that would be missed if only free thyroxine were determined. With both free-thyroxine methods, the values distinguished hyperthyroid patients from normal controls and pregnant women with 100% accuracy, but there was some overlap between hypothyroid patients and controls. Absolute values with the kit procedure often exceed those obtained by dialysis, especially for hypothyroid patients and pregnant women. We conclude that the kit may be of as much diagnostic value as the dialysis method if the limitations regarding absolute values are kept in mind and the test is not used as a substitute for thyrotropin determinations in cases of suspected hypothyroidism.

Determination of cis-diamminedichloroplatinum (II) in plasma proteins and hemoglobin of cancer patients

1989 ◽  
Vol 63 (5) ◽  
pp. 361-366 ◽  
Author(s):  
Riitta Mustonen ◽  
P�ivi Hietanen ◽  
Sinikka Lepp�l� ◽  
Mervi Takala ◽  
Kari Hemminki
Keyword(s):  
Cancer Patients ◽  
Plasma Proteins

Binding of calcium by human plasma proteins under simulated physiologic conditions

1964 ◽  
Vol 19 (2) ◽  
pp. 292-296 ◽  
Author(s):  
Irene R. Held ◽  
Smith Freeman
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Protein Concentration ◽  
Calcium Concentration ◽  
Gamma Globulin ◽  
Chloride Concentration ◽  
Total Calcium ◽  
Total Protein Concentration ◽  
Plasma Albumin

The binding of calcium to human plasma albumin, alpha, beta, and gamma globulins was studied with the aid of an ultracentrifuge. The amount of calcium bound to these separated proteins was determined in solutions with electrolyte concentrations and pH within physiological ranges. The total calcium concentration was 2.35–2.90 mm/liter H2O and the total protein concentration was 3.91–4.29 g/100 ml H2O. In these solutions no significant differences were found for the binding of calcium (expressed as mm Ca++ bound per gram protein) by albumin, alpha, and beta globulins; the average values obtained were, respectively, 0.016, 0.018, and 0.023. Significantly less calcium was bound by gamma globulin; 0.009 mm/gram. The pH was varied between 7.200–7.550 and the sodium chloride concentration between 114–157 mEq Na per liter. These changes did not measurably affect the amount of calcium bound to albumin. protein-bound calcium; ultracentrifugation and determination of protein-bound calcium; plasma globulin-bound calcium; plasma albumin-bound calcium Submitted on July 2, 1963

Radioenzymic determination of homocysteine in plasma and urine.

1985 ◽  
Vol 31 (4) ◽  
pp. 624-628 ◽  
Author(s):  
H Refsum ◽  
S Helland ◽  
P M Ueland
Keyword(s):  
Plasma Proteins ◽  
High Performance ◽  
Gel Filtration ◽  
Strong Acid ◽  
High Performance Liquid Chromatographic ◽  
Total Homocysteine ◽  
Liquid Chromatographic ◽  
Fraction Bound

Abstract Using a modification of the radioenzymic assay described previously (J Biol Chem 259: 2360-2364, 1984) we measured homocysteine in freshly prepared plasma and urine from volunteers. The concentration of free homocysteine--i.e., the amount measurable in plasma after deproteinization by strong acid--was 2.27 (SEM 0.11) mumol/L for 18 men and 1.95 (SEM 0.13) mumol/L for 16 women (p greater than 0.05, not significant). About 70% of the total homocysteine in human plasma was associated with plasma proteins, and was precipitated with strong acid. The concentration of protein-bound homocysteine in plasma was 6.51 (SEM 0.32) mumol/L for men and 7.29 (SEM 0.65) mumol/L for women, a significantly (p less than 0.01) different spread. Homocysteine was rapidly released from plasma proteins in the presence of a reducing agent, dithioerythritol. By gel filtration of plasma on a "high-performance" liquid-chromatographic column, albumin was shown to be the sole carrier of homocysteine in plasma. Because the fraction bound to protein as determined by this procedure equaled that obtained by precipitation of plasma proteins with acid, we conclude that homocysteine is bound to albumin in vivo. The concentration of homocysteine in urine ranged from 3.5 to 9.5 mumol/L, about 6 mumol of homocysteine being excreted per 24 h.

scholarly journals Plasma Cortisone in Man: Its Determination, Physiological Variation, and Significance

1980 ◽  
Vol 17 (5) ◽  
pp. 227-232 ◽  
Author(s):  
J D Few ◽  
G C Cashmore
Keyword(s):  
Protein Binding ◽  
Simultaneous Determination ◽  
Cortisol Level ◽  
Paper Chromatography ◽  
Plasma Proteins ◽  
Hepatic Uptake ◽  
Physiological Variation ◽  
Competitive Protein Binding ◽  
Response To Exercise

In a method for the simultaneous determination of cortisone, cortisol, and corticosterone, the extracted steroids are separated using paper chromatography and assayed by competitive protein binding. Evidence of the reliability of the method, particularly with respect to the determination of cortisone, is presented. Only trivial changes in cortisone level were detected in response to exercise, surgery, and ACTH, even though marked changes in cortisol level were simultaneously recorded. It is suggested that the inertia in plasma cortisone level may be related to its lesser degree of binding to plasma proteins, relative to cortisol, which would permit more rapid hepatic uptake and possible accumulation of a large extravascular pool of cortisone.

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