PROTEIN-BORONIC ACID CONJUGATES AND THEIR BINDING TO LOW-MOLECULAR-MASS CIS-DIOLS AND GLYCATED HEMOGLOBIN

被引：42

作者：

FRANTZEN, F ^{[1
]}

GRIMSRUD, K ^{[1
]}

HEGGLI, DE ^{[1
]}

SUNDREHAGEN, E ^{[1
]}

机构：

[1] AXIS BIOCHEM AS,N-0505 OSLO,NORWAY

来源：

JOURNAL OF CHROMATOGRAPHY B-BIOMEDICAL APPLICATIONS | 1995年 / 670卷 / 01期

关键词：

D O I：

10.1016/0378-4347(95)00141-5

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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, were tested for their binding of D-sorbitol, D-mannose and glycohemoglobin (GHb). Similarly, alkaline phosphatase-PBA conjugates were used in an attempted enzyme-linked sorbent assay for the detection of GHb. Affinity chromatography on immobilised D-mannose and gel chromatographic studies of protein-PEA complexes with [C-14]sorbitol, clearly illustrated a low affinity of the interaction studied. Glycated hemoglobin could not be detected using the enzyme-linked sorbent assay approach. However, GHb was found to be specifically retained on columns filled with protein-PEA-coated particles as affinity matrix, enabling the glycation level of blood samples to be determined.

引用

页码：37 / 45

页数：9

共 28 条

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