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

Research output: Contribution to journalArticle

11 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1069-1074
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume115
Issue number3
DOIs
StatePublished - Sep 30 1983

Fingerprint

Electrophoresis
Lectins
Cations
Metal ions
Metals
Ions
Native Polyacrylamide Gel Electrophoresis
Divalent Cations
Gels
Carbohydrates

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Dependence on cations for the binding activity of lectins as determined by affinity electrophoresis. / Lönnerdal, Bo; Borrebaeck, Carl A K; Etzler, Marilynn E.; Ersson, Bo.

In: Biochemical and Biophysical Research Communications, Vol. 115, No. 3, 30.09.1983, p. 1069-1074.

Research output: Contribution to journalArticle

Lönnerdal, Bo ; Borrebaeck, Carl A K ; Etzler, Marilynn E. ; Ersson, Bo. / Dependence on cations for the binding activity of lectins as determined by affinity electrophoresis. In: Biochemical and Biophysical Research Communications. 1983 ; Vol. 115, No. 3. pp. 1069-1074.
@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 = "9",
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 -