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 › peer-review

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

Access to Document

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

Fingerprint Dive into the research topics of 'Dependence on cations for the binding activity of lectins as determined by affinity electrophoresis'. Together they form a unique fingerprint.

Cite this

@article{49aad804f2304edc80955c6a18192a5d,

title = "Dependence on cations for the binding activity of lectins as determined by affinity electrophoresis",

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.",

author = "Bo L{\"o}nnerdal and Borrebaeck, {Carl A K} and Etzler, {Marilynn E.} and Bo Ersson",

year = "1983",

month = sep,

day = "30",

doi = "10.1016/S0006-291X(83)80044-8",

language = "English (US)",

volume = "115",

pages = "1069--1074",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Dependence on cations for the binding activity of lectins as determined by affinity electrophoresis

AU - Lönnerdal, Bo

AU - Borrebaeck, Carl A K

AU - Etzler, Marilynn E.

AU - Ersson, Bo

PY - 1983/9/30

Y1 - 1983/9/30

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0021115970&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021115970&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(83)80044-8

DO - 10.1016/S0006-291X(83)80044-8

M3 - Article

C2 - 6626217

AN - SCOPUS:0021115970

VL - 115

SP - 1069

EP - 1074

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this