Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

Changes in intrinsic circular dichroism of several homogeneous anti-type 3 pneumococcal antibodies on binding of a small hapten

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Holowka, D. A.
  • Strosberg, Donny
  • Kimball, J. W.
  • Haber, E.
  • Cathou, R. E.

publication date

  • 1972

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Three homogeneous antibodies against the capsular polysaccharide of Type III pneumococci of similar specificities and affinities were purified from a single bleeding of an individual rabbit and fractionated by isoelectric focusing. A comparison of the circular dichroic spectra of the three antibodies revealed differences among them, although the spectra were generally similar to those obtained previously for heterogeneous rabbit antibodies [Cathou, R. E., Kulcycki, A., Jr. & Haber, E. (1968) Biochemistry 7, 3958]. On binding of the hexasaccharide, -[-->3)-beta-D-glucuronic acid-(1-->4)-beta-D-glucose-(1-](3)-->, significant changes in all three circular dichroic spectra were observed. Since the oligosaccharide alone shows no transitions above 220 nm, these spectral changes can be attributed to changes in the intrinsic optical activity of the antibodies. Calculated difference circular dichroism spectra (of antibody minus that of antibody-hapten complex) of the three antibodies are different from each other, and resemble spectra of tryptophan and tyrosine derivatives. These changes in optical activity can be ascribed to changes in the asymmetric environments of aromatic chromophores directly in the combining site and/or to changes in orientation inside or beyond the site. Since the hapten-antibody interactions are different in the three antibodies, as shown by the difference spectra, the structures of the combining sites are presumably also different. We have interpreted these observations to mean that a relatively simple ligand may be bound by several different complementary sites.

subject areas

  • Animals
  • Antibodies
  • Antibodies, Bacterial
  • Antigen-Antibody Reactions
  • Binding Sites, Antibody
  • Circular Dichroism
  • Electrophoresis, Polyacrylamide Gel
  • Haptens
  • Isoelectric Focusing
  • Polysaccharides, Bacterial
  • Protein Conformation
  • Rabbits
  • Spectrum Analysis
  • Streptococcus pneumoniae
scroll to property group menus

Identity

PubMed Central ID

  • PMC389779

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.69.11.3399

PubMed ID

  • 4404497
scroll to property group menus

Additional Document Info

start page

  • 3399

end page

  • 3403

volume

  • 69

issue

  • 11

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support