Homogeneous enzyme-linked competitive binding assay for riboflavin

Solid phase enzyme-linked competitive binding assay for riboflavin.

A new solid-phase enzyme-linked assay for riboflavin (vitamin B2) is described. The assay is based on the competition between analyte vitamin molecules and a glucose-6-phosphate dehydrogenase-3-carboxymethylriboflavin conjugate for a limited number of riboflavin-binding protein sites immobilized on Sepharose particles. Significant improvements in conjugate catalytic activity and thus detectabil...

H9mogeneous Enzyme-linked Competitive Binding Assay for Riboflavin

A rapid and precise homogeneous enzyme-linked competitive binding assay for riboflavin (vitamin Bz) is described. The method utilizes a malate dehydrogenase/3-carboxymethylriboflavin conjugate in conjunction with soluble riboflavin binding protein. In the absence of the vitamin, the catalytic activity of the enzyme/riboflavin conjugate is inhibited up to 71% by the binding protein. In the prese...

Enzyme-Linked Immunosorbent Assay Competitive Binding Inhibition

Homogeneous Enzyme-linked Competitive Binding Assay for Biotin Based on the Avidin-biotin Interaction

A homogeneous enzyme-linked competitive-binding assay for biotin with glucose-6-phosphate dehydrogenase (GGPDH), is described. This assay is based on the interaction between a GGPDH/biotin conjugate with avidin, a natural binder for biotin. In the absence of biotin in the assay mixture, this interaction results in 100% inhibition of the enzyme conjugate. In the presence of biotin, the enzymatic...

ENZYME-LINKED IMMUNOSORBENT ASSAY OF NEOPTERIN USING PENICILLINASE AS LABEL

An enzyme-linked immunosorbent assay for neopterin using penicillinase as marker enzyme is reported here by polyclonal antibodies against neopterin conjugated to bovine serum albumin which were raised in rabbits. Immunoglobulin fractions were purified and coated on wells of microtiter plates. A chain heterology was introduced in neopterin derivative and conjugated to penicillinase. The assa...