Dependence on cations for the binding activity of lectins as determined by affinity electrophoresis

Bo Lönnerdal; Carl A K Borrebaeck; Marilynn E. Etzler; Bo Ersson

doi:10.1016/S0006-291X(83)80044-8

Dependence on cations for the binding activity of lectins as determined by affinity electrophoresis

Bo Lönnerdal, Carl A K Borrebaeck, Marilynn E. Etzler, Bo Ersson

Endocrinology, Diabetes, and Metabolism

Research output: Contribution to journal › Article

11 Scopus citations

Abstract

The metal ion content of eighteen different lectins was determined. The lectins were demetallized and the binding activity of native and demetallized forms were investigated using non-denaturing polyacrylamide affinity gel electrophoresis. The binding activities of all lectins were dependent on their metal ion content; when the cations were removed the lectins lost their carbohydrate binding activity. There was a marked difference in the strength with which lectins bind divalent cations.

Original language	English (US)
Pages (from-to)	1069-1074
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	115
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(83)80044-8
State	Published - Sep 30 1983

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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abstract = "The metal ion content of eighteen different lectins was determined. The lectins were demetallized and the binding activity of native and demetallized forms were investigated using non-denaturing polyacrylamide affinity gel electrophoresis. The binding activities of all lectins were dependent on their metal ion content; when the cations were removed the lectins lost their carbohydrate binding activity. There was a marked difference in the strength with which lectins bind divalent cations.",

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AB - The metal ion content of eighteen different lectins was determined. The lectins were demetallized and the binding activity of native and demetallized forms were investigated using non-denaturing polyacrylamide affinity gel electrophoresis. The binding activities of all lectins were dependent on their metal ion content; when the cations were removed the lectins lost their carbohydrate binding activity. There was a marked difference in the strength with which lectins bind divalent cations.

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