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Title: Detergent activation of the binding protein in the folate radioassay

Journal Article · · Clin. Chem. (Winston-Salem, N.C.); (United States)
OSTI ID:5761057

A minor cow's whey protein associated with ..beta..-lactoglobulin is used as binding protein in the competitive radioassay for serum and erythrocyte folate. Seeking to optimize the assay, we tested the performance of binder solutions of increasing purity. The folate binding protein was isolated from cow's whey by means of CM-Sepharose CL-6B cation-exchange chromatography, and further purified on a methotrexate-AH-Sepharose 4B affinity matrix. In contrast to ..beta..-lactoglobulin, the purified protein did not bind folate unless the detergents cetyltrimethylammonium (10 mmol/Ll) or Triton X-100 (1 g/L) were present. Such detergent activation was not needed in the presence of serum. There seems to be a striking analogy between these phenomena and the well-known reactivation of certain purified membrane-derived enzymes by surfactants (lipids/detergents).

OSTI ID:
5761057
Journal Information:
Clin. Chem. (Winston-Salem, N.C.); (United States), Vol. 28:1
Country of Publication:
United States
Language:
English