METAL ION REQUIREMENTS OF CONCANAVALIN A.

A. D. Sherry, A. D. Newman

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Concanavalin A, the lectin or plant hemagglutinin obtained from Canavalia ensiformis, contains the metals manganese and calcium in its native state. Several workers have shown that the protein has two transition metal binding sites (S1) and two calcium ion binding sites (S2) per dimer of molecular weight 53,000 (1-3). The protein must have a full complement of these metal ions for optimal binding of saccharides. Earlier, water proton relaxation rate and fluorescence titrations gave evidence of two strong and two weak lanthanide binding sites per dimer of apo-concanavalin A. These studies suggested that the lanthanide ions not only substitute for calcium in S2 but also bind at S1 with an association constant similar to that of manganese. The paper reports the effects of the substitution of these ions upon the proteins' ability to bind saccharides.

Original languageEnglish (US)
Title of host publicationUnknown Host Publication Title
Place of PublicationOak Ridge, Tenn
PublisherAEC
Pages213-217
Number of pages5
StatePublished - 1800
EventRare Earth Res Conf, 11th, Proc - Traverse City, MI, USA
Duration: Oct 7 1974Oct 10 1974

Other

OtherRare Earth Res Conf, 11th, Proc
CityTraverse City, MI, USA
Period10/7/7410/10/74

Fingerprint

Binding sites
Metal ions
Calcium
Rare earth elements
Proteins
Dimers
Manganese
Ions
Titration
Transition metals
Protons
Substitution reactions
Fluorescence
Molecular weight
Association reactions
Metals
Water

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Sherry, A. D., & Newman, A. D. (1800). METAL ION REQUIREMENTS OF CONCANAVALIN A. In Unknown Host Publication Title (pp. 213-217). Oak Ridge, Tenn: AEC.

METAL ION REQUIREMENTS OF CONCANAVALIN A. / Sherry, A. D.; Newman, A. D.

Unknown Host Publication Title. Oak Ridge, Tenn : AEC, 1800. p. 213-217.

Research output: Chapter in Book/Report/Conference proceedingChapter

Sherry, AD & Newman, AD 1800, METAL ION REQUIREMENTS OF CONCANAVALIN A. in Unknown Host Publication Title. AEC, Oak Ridge, Tenn, pp. 213-217, Rare Earth Res Conf, 11th, Proc, Traverse City, MI, USA, 10/7/74.
Sherry AD, Newman AD. METAL ION REQUIREMENTS OF CONCANAVALIN A. In Unknown Host Publication Title. Oak Ridge, Tenn: AEC. 1800. p. 213-217
Sherry, A. D. ; Newman, A. D. / METAL ION REQUIREMENTS OF CONCANAVALIN A. Unknown Host Publication Title. Oak Ridge, Tenn : AEC, 1800. pp. 213-217
@inbook{6ac54e82b1744e2b9d8ef13d79d1a1c6,
title = "METAL ION REQUIREMENTS OF CONCANAVALIN A.",
abstract = "Concanavalin A, the lectin or plant hemagglutinin obtained from Canavalia ensiformis, contains the metals manganese and calcium in its native state. Several workers have shown that the protein has two transition metal binding sites (S1) and two calcium ion binding sites (S2) per dimer of molecular weight 53,000 (1-3). The protein must have a full complement of these metal ions for optimal binding of saccharides. Earlier, water proton relaxation rate and fluorescence titrations gave evidence of two strong and two weak lanthanide binding sites per dimer of apo-concanavalin A. These studies suggested that the lanthanide ions not only substitute for calcium in S2 but also bind at S1 with an association constant similar to that of manganese. The paper reports the effects of the substitution of these ions upon the proteins' ability to bind saccharides.",
author = "Sherry, {A. D.} and Newman, {A. D.}",
year = "1800",
language = "English (US)",
pages = "213--217",
booktitle = "Unknown Host Publication Title",
publisher = "AEC",

}

TY - CHAP

T1 - METAL ION REQUIREMENTS OF CONCANAVALIN A.

AU - Sherry, A. D.

AU - Newman, A. D.

PY - 1800

Y1 - 1800

N2 - Concanavalin A, the lectin or plant hemagglutinin obtained from Canavalia ensiformis, contains the metals manganese and calcium in its native state. Several workers have shown that the protein has two transition metal binding sites (S1) and two calcium ion binding sites (S2) per dimer of molecular weight 53,000 (1-3). The protein must have a full complement of these metal ions for optimal binding of saccharides. Earlier, water proton relaxation rate and fluorescence titrations gave evidence of two strong and two weak lanthanide binding sites per dimer of apo-concanavalin A. These studies suggested that the lanthanide ions not only substitute for calcium in S2 but also bind at S1 with an association constant similar to that of manganese. The paper reports the effects of the substitution of these ions upon the proteins' ability to bind saccharides.

AB - Concanavalin A, the lectin or plant hemagglutinin obtained from Canavalia ensiformis, contains the metals manganese and calcium in its native state. Several workers have shown that the protein has two transition metal binding sites (S1) and two calcium ion binding sites (S2) per dimer of molecular weight 53,000 (1-3). The protein must have a full complement of these metal ions for optimal binding of saccharides. Earlier, water proton relaxation rate and fluorescence titrations gave evidence of two strong and two weak lanthanide binding sites per dimer of apo-concanavalin A. These studies suggested that the lanthanide ions not only substitute for calcium in S2 but also bind at S1 with an association constant similar to that of manganese. The paper reports the effects of the substitution of these ions upon the proteins' ability to bind saccharides.

UR - http://www.scopus.com/inward/record.url?scp=0016408582&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0016408582&partnerID=8YFLogxK

M3 - Chapter

SP - 213

EP - 217

BT - Unknown Host Publication Title

PB - AEC

CY - Oak Ridge, Tenn

ER -