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 | |
| State | Published - Sep 30 1983 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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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 journal › Article
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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 -