F. Frantzen et al., PROTEIN-BORONIC ACID CONJUGATES AND THEIR BINDING TO LOW-MOLECULAR-MASS CIS-DIOLS AND GLYCATED HEMOGLOBIN, Journal of chromatography B. Biomedical applications, 670(1), 1995, pp. 37-45
Citations number
28
Categorie Soggetti
Chemistry Analytical","Biochemical Research Methods
Journal title
Journal of chromatography B. Biomedical applications
Different methods for covalent linkage of phenylboronic acid (PEA) to
structural proteins and enzymes are presented. Protein-PEA conjugates,
free in solution or immobilised on magnetizable polymer particles, we
re tested for their binding of D-sorbitol, D-mannose and glycohemoglob
in (GHb). Similarly, alkaline phosphatase-PBA conjugates were used in
an attempted enzyme-linked sorbent assay for the detection of GHb. Aff
inity chromatography on immobilised D-mannose and gel chromatographic
studies of protein-PEA complexes with [C-14]sorbitol, clearly illustra
ted a low affinity of the interaction studied. Glycated hemoglobin cou
ld not be detected using the enzyme-linked sorbent assay approach. How
ever, GHb was found to be specifically retained on columns filled with
protein-PEA-coated particles as affinity matrix, enabling the glycati
on level of blood samples to be determined.