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Covalent and 3-dimensional structure of concanavalin-a .1. Amino-acid sequence of cyanogen-bromide fragments f1 and f2

Academic Article
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Overview

authors

  • Wang, J. L.
  • Cunningham, Bruce
  • Waxdal, M. J.
  • Edelman, Gerald

publication date

  • 1975

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Concanavalin A is a lectin composed of identical subunits, each containg 237 amino acid residues. The complete amino acid sequence of the first 129 residues of the polypeptide chain has been determined by analysis of peptides obtained from digests of CNBr Fragments F1 (residues 1 to 42) and F2 (residues 40 to 129). Correlation of the chemical sequence with x-ray crystallographic results indicates that Fragment F1 contains all of the protein ligands for the binding of 2 metal ions, Mn2+ and Ca2+, and that Fragment F2 contains many of the residues involved in the interactions of the subunits to form dimers and tetramers. The site of cleavage of the polypeptide chain to yield the naturally occurring Fragments A1 and A2 has also been identified as the peptide bond between residues 118 and 119.

subject areas

  • Amino Acid Sequence
  • Amino Acids
  • Binding Sites
  • Calcium
  • Carboxypeptidases
  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel
  • Chymotrypsin
  • Concanavalin A
  • Cyanogen Bromide
  • Leucyl Aminopeptidase
  • Manganese
  • Peptide Fragments
  • Protein Binding
  • Protein Conformation
  • Thermolysin
  • Trypsin
  • X-Ray Diffraction
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 1112813
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Additional Document Info

start page

  • 1490

end page

  • 1502

volume

  • 250

issue

  • 4

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