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A competitive protein-binding assay for 25-hydroxyvitamin D.

J M Pettifor, F P Ross, J Wang

Clinical Science and Molecular Medicine

|December 1, 1976

Summary

This study presents a new assay for measuring 25-hydroxyvitamin D (25(OH)D) without separating it from vitamin D. The assay utilizes bovine albumin and provides reliable 25(OH)D levels in children.

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Area of Science:

Biochemistry
Clinical Chemistry
Endocrinology

Background:

Accurate measurement of 25-hydroxyvitamin D (25(OH)D) is crucial for assessing vitamin D status.
Existing assays often require complex separation steps for vitamin D and its metabolites.
Variability in assay components, such as bovine albumin, can significantly impact results.

Purpose of the Study:

To develop and validate a modified competitive protein-binding assay for 25(OH)D.
To eliminate the need for prior separation of vitamin D from 25(OH)D.
To establish reference ranges for 25(OH)D in a pediatric population.

Main Methods:

A modified competitive protein-binding assay was developed for 25(OH)D.
Bovine albumin was employed as a protein stabilizer and lipid solubilizer at 1 mg/ml.
The impact of different bovine albumin sources on non-specific binding of 25-(3H)hydroxycholecalciferol was evaluated.

Main Results:

The assay successfully measured 25(OH)D without requiring prior separation from vitamin D.
Significant variations in non-specific binding were observed with bovine albumin from different manufacturers (3.3% to 58.9%).
The mean serum 25(OH)D concentration in normal children from Johannesburg was determined to be 76.75 ± 24.75 µmol/ml (30.7 ± 9.9 ng/ml).

Conclusions:

The modified assay offers a simpler method for quantifying 25(OH)D.
Careful selection of bovine albumin is critical to minimize assay variability.
The established reference range provides valuable data for pediatric vitamin D assessment in the region.

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