Interactions of saccharides with concanavalin A. Relation between calcium ions and the binding of saccharides to concanavalin A

Curtis F. Brewer, D. M. Marcus, A. P. Grollman, H. Sternlicht

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

Previous studies were interpreted as showing that transition metal and calcium ions must be bound to concanavalin A before this lectin can bind sugars. In contrast, it was found that the addition of calcium ions fails to affect the following properties of manganese concanavalin A if the metalloprotein is prepared in their presence: electron spin resonance spectrum of the manganese ion in the protein; spin lattice relaxation time of solvent water protons measured in the presence of the protein; and spin lattice and transverse relaxation times of the 13C carbons of α methyl D glucopyranoside (uniformly enriched with 14% 13C) in the presence of manganese concanavalin A. These results indicate that saccharide binding activity of the protein is independent of calcium ion binding if a transition metal ion (Mn2+) initially binds to the protein in the presence of calcium ions. The role of calcium ion binding to concanavalin A appears to be that of accelerating the rate of formation of the final transition metal protein complex.

Original languageEnglish (US)
Pages (from-to)4614-4616
Number of pages3
JournalJournal of Biological Chemistry
Volume249
Issue number14
StatePublished - 1974

Fingerprint

Concanavalin A
Ions
Calcium
Manganese
Transition metals
Proteins
Relaxation time
Metalloproteins
Metals
Spin-lattice relaxation
Lectins
Sugars
Coordination Complexes
Electron Spin Resonance Spectroscopy
Metal ions
Paramagnetic resonance
Protons
Carbon
Water

ASJC Scopus subject areas

  • Biochemistry

Cite this

Interactions of saccharides with concanavalin A. Relation between calcium ions and the binding of saccharides to concanavalin A. / Brewer, Curtis F.; Marcus, D. M.; Grollman, A. P.; Sternlicht, H.

In: Journal of Biological Chemistry, Vol. 249, No. 14, 1974, p. 4614-4616.

Research output: Contribution to journalArticle

@article{9e0e9c1e42e949e9a1efb69e564a1c32,
title = "Interactions of saccharides with concanavalin A. Relation between calcium ions and the binding of saccharides to concanavalin A",
abstract = "Previous studies were interpreted as showing that transition metal and calcium ions must be bound to concanavalin A before this lectin can bind sugars. In contrast, it was found that the addition of calcium ions fails to affect the following properties of manganese concanavalin A if the metalloprotein is prepared in their presence: electron spin resonance spectrum of the manganese ion in the protein; spin lattice relaxation time of solvent water protons measured in the presence of the protein; and spin lattice and transverse relaxation times of the 13C carbons of α methyl D glucopyranoside (uniformly enriched with 14{\%} 13C) in the presence of manganese concanavalin A. These results indicate that saccharide binding activity of the protein is independent of calcium ion binding if a transition metal ion (Mn2+) initially binds to the protein in the presence of calcium ions. The role of calcium ion binding to concanavalin A appears to be that of accelerating the rate of formation of the final transition metal protein complex.",
author = "Brewer, {Curtis F.} and Marcus, {D. M.} and Grollman, {A. P.} and H. Sternlicht",
year = "1974",
language = "English (US)",
volume = "249",
pages = "4614--4616",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "14",

}

TY - JOUR

T1 - Interactions of saccharides with concanavalin A. Relation between calcium ions and the binding of saccharides to concanavalin A

AU - Brewer, Curtis F.

AU - Marcus, D. M.

AU - Grollman, A. P.

AU - Sternlicht, H.

PY - 1974

Y1 - 1974

N2 - Previous studies were interpreted as showing that transition metal and calcium ions must be bound to concanavalin A before this lectin can bind sugars. In contrast, it was found that the addition of calcium ions fails to affect the following properties of manganese concanavalin A if the metalloprotein is prepared in their presence: electron spin resonance spectrum of the manganese ion in the protein; spin lattice relaxation time of solvent water protons measured in the presence of the protein; and spin lattice and transverse relaxation times of the 13C carbons of α methyl D glucopyranoside (uniformly enriched with 14% 13C) in the presence of manganese concanavalin A. These results indicate that saccharide binding activity of the protein is independent of calcium ion binding if a transition metal ion (Mn2+) initially binds to the protein in the presence of calcium ions. The role of calcium ion binding to concanavalin A appears to be that of accelerating the rate of formation of the final transition metal protein complex.

AB - Previous studies were interpreted as showing that transition metal and calcium ions must be bound to concanavalin A before this lectin can bind sugars. In contrast, it was found that the addition of calcium ions fails to affect the following properties of manganese concanavalin A if the metalloprotein is prepared in their presence: electron spin resonance spectrum of the manganese ion in the protein; spin lattice relaxation time of solvent water protons measured in the presence of the protein; and spin lattice and transverse relaxation times of the 13C carbons of α methyl D glucopyranoside (uniformly enriched with 14% 13C) in the presence of manganese concanavalin A. These results indicate that saccharide binding activity of the protein is independent of calcium ion binding if a transition metal ion (Mn2+) initially binds to the protein in the presence of calcium ions. The role of calcium ion binding to concanavalin A appears to be that of accelerating the rate of formation of the final transition metal protein complex.

UR - http://www.scopus.com/inward/record.url?scp=0016213530&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016213530&partnerID=8YFLogxK

M3 - Article

VL - 249

SP - 4614

EP - 4616

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 14

ER -