Competitive protein binding assay for activin AEDF using follistatin determination of activin levels in human plasma

Abstract A Porter and Silber procedure, a fluorometric procedure, a double-isotope derivative procedure, and a competitive protein-binding assay procedure were used to determine 17-hydroxycorticosteroids in plasma from normal individuals and from patients with endocrinopathies. Results from each of these procedures were intercompared. Results of the fluorometric procedure and the competitive protein-binding assay compared favorably with results obtained by the more elaborate and difficult double-isotope derivative method. The Porter and Silber method is less specific. This study should be a useful aid in comparing values with those of other laboratories and in selecting the most advantageous method for use by a particular laboratory.

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Nonsuppressible Insulin-Like Activity (NSILA). I. Development of New Sensitive Competitive Protein-Binding Assay for Determination of Serum Levels*

The Journal of Clinical Endocrinology & Metabolism ◽

10.1210/jcem-46-4-664 ◽

1978 ◽

Vol 46 (4) ◽

pp. 664-671 ◽

Cited By ~ 29

Author(s):

DON S. SCHALCH ◽

UDO E. HEINRICH ◽

JANET G. KOCH ◽

CAROLYN J. JOHNSON ◽

ROBERT J. SCHLUETER

Keyword(s):

Protein Binding ◽

Binding Assay ◽

Serum Levels ◽

Protein Binding Assay ◽

Competitive Protein Binding Assay ◽

Competitive Protein Binding ◽

Insulin Like Activity

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Modification of a Competitive Protein Binding Assay for Determination of Inositol 1,4,5-Trisphosphate

Analytical Biochemistry ◽

10.1006/abio.1993.1148 ◽

1993 ◽

Vol 210 (1) ◽

pp. 45-49 ◽

Cited By ~ 13

Author(s):

P. Gerwins

Keyword(s):

Protein Binding ◽

Binding Assay ◽

Protein Binding Assay ◽

Inositol 1,4,5 Trisphosphate ◽

Competitive Protein Binding Assay ◽

Competitive Protein Binding

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Comparison of a Fluorimetric Method and a Competitive Protein Binding Assay Kit for the Determination of Plasma Hydroxycorticosteroids

Annals of Clinical Biochemistry International Journal of Laboratory Medicine ◽

10.1177/000456327501200138 ◽

1975 ◽

Vol 12 (1-6) ◽

pp. 160-162 ◽

Cited By ~ 9

Author(s):

Marion Gore ◽

Eva Lester

Keyword(s):

Protein Binding ◽

Binding Assay ◽

Normal Subjects ◽

Fluorimetric Method ◽

Protein Binding Assay ◽

Competitive Protein Binding Assay ◽

Competitive Protein Binding ◽

The Mean ◽

Selenium 75

A new competitive protein binding (C.P.B.) assay kit for the determination of plasma hydroxycorticosteroids which uses a gamma emitting isotope, selenium-75, to label the Cortisol was compared with a fluorimetric method in use in a routine laboratory. The mean plasma corticosteroid level in a group of 54 normal subjects was found to be lower with the C.P.B. kit than with the fluorimetric method. The correlation coefficient between the two methods in 131 specimens from healthy subjects and patients under investigation for pituitary or adrenocortical disorders was + 0.92. The precision of the two methods was similar.

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Determination of erythrocyte folate by competitive protein binding assay preceded by extraction.

Clinical Chemistry ◽

10.1093/clinchem/22.7.982 ◽

1976 ◽

Vol 22 (7) ◽

pp. 982-992 ◽

Cited By ~ 10

Author(s):

E Mortensen

Keyword(s):

Protein Binding ◽

Binding Assay ◽

Extraction Procedure ◽

Molecular Configuration ◽

Protein Binding Assay ◽

Competitive Protein Binding Assay ◽

Competitive Protein Binding ◽

Erythrocyte Folate

Abstract Determination of the concentration of erythrocyte folate by means of competitive protein binding assay critically depends on the extraction procedure applied. Results will be influenced by variable factors such as the in vitro age of the blood samples, the degree of hemolysis, the presence of ascorbic acid, and the pH during extraction and elimination of proteins. The radioassay is strongly influenced by the pH of the final reaction mixture, the method used to separate free and protein-bound molecules, and the molecular configuration of the folates present. Based on experimental results presented, I describe a method for the determination of erythrocyte folate.

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