Circular dichroism studies of cobalt substituted lentil lectin

Emilie Stafford, W. David Behnke, Lokesh Bhattacharyya, Curtis F. Brewer

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A recent method has been developed to effect metal ion substitution at the Mn2+ site in the lentil lectin (Bhattacharyya et al. (1984) Biochem. Biophys. Res. Commun. 124, 857-862). We report here the preparation of cobalt substituted lentil lectin, containing Co2+ at the S1 site and Ca2+ at the S2 site. The cobalt derivative possesses full saccharide binding activity and can be used for spectroscopic studies. The near UV and visible CD spectra of the derivative are shown, and its spectral properties are compared with various cobalt complexes of concanavalin A.

Original languageEnglish (US)
Pages (from-to)438-444
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume136
Issue number1
DOIs
StatePublished - Apr 14 1986

Fingerprint

Circular Dichroism
Cobalt
Derivatives
Concanavalin A
Metal ions
Substitution reactions
Metals
Ions
lentil lectin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Circular dichroism studies of cobalt substituted lentil lectin. / Stafford, Emilie; Behnke, W. David; Bhattacharyya, Lokesh; Brewer, Curtis F.

In: Biochemical and Biophysical Research Communications, Vol. 136, No. 1, 14.04.1986, p. 438-444.

Research output: Contribution to journalArticle

Stafford, Emilie ; Behnke, W. David ; Bhattacharyya, Lokesh ; Brewer, Curtis F. / Circular dichroism studies of cobalt substituted lentil lectin. In: Biochemical and Biophysical Research Communications. 1986 ; Vol. 136, No. 1. pp. 438-444.
@article{73e55be333bf4ed4aa719480f1fe2fb8,
title = "Circular dichroism studies of cobalt substituted lentil lectin",
abstract = "A recent method has been developed to effect metal ion substitution at the Mn2+ site in the lentil lectin (Bhattacharyya et al. (1984) Biochem. Biophys. Res. Commun. 124, 857-862). We report here the preparation of cobalt substituted lentil lectin, containing Co2+ at the S1 site and Ca2+ at the S2 site. The cobalt derivative possesses full saccharide binding activity and can be used for spectroscopic studies. The near UV and visible CD spectra of the derivative are shown, and its spectral properties are compared with various cobalt complexes of concanavalin A.",
author = "Emilie Stafford and Behnke, {W. David} and Lokesh Bhattacharyya and Brewer, {Curtis F.}",
year = "1986",
month = "4",
day = "14",
doi = "10.1016/0006-291X(86)90930-7",
language = "English (US)",
volume = "136",
pages = "438--444",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Circular dichroism studies of cobalt substituted lentil lectin

AU - Stafford, Emilie

AU - Behnke, W. David

AU - Bhattacharyya, Lokesh

AU - Brewer, Curtis F.

PY - 1986/4/14

Y1 - 1986/4/14

N2 - A recent method has been developed to effect metal ion substitution at the Mn2+ site in the lentil lectin (Bhattacharyya et al. (1984) Biochem. Biophys. Res. Commun. 124, 857-862). We report here the preparation of cobalt substituted lentil lectin, containing Co2+ at the S1 site and Ca2+ at the S2 site. The cobalt derivative possesses full saccharide binding activity and can be used for spectroscopic studies. The near UV and visible CD spectra of the derivative are shown, and its spectral properties are compared with various cobalt complexes of concanavalin A.

AB - A recent method has been developed to effect metal ion substitution at the Mn2+ site in the lentil lectin (Bhattacharyya et al. (1984) Biochem. Biophys. Res. Commun. 124, 857-862). We report here the preparation of cobalt substituted lentil lectin, containing Co2+ at the S1 site and Ca2+ at the S2 site. The cobalt derivative possesses full saccharide binding activity and can be used for spectroscopic studies. The near UV and visible CD spectra of the derivative are shown, and its spectral properties are compared with various cobalt complexes of concanavalin A.

UR - http://www.scopus.com/inward/record.url?scp=0023048479&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023048479&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(86)90930-7

DO - 10.1016/0006-291X(86)90930-7

M3 - Article

C2 - 3707581

AN - SCOPUS:0023048479

VL - 136

SP - 438

EP - 444

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -