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Binding and functional properties of concanavalin-a and its derivatives .2. Proteolytic product with saccharide-binding activity

Academic Article
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Overview

authors

  • Wang, J. L.
  • Edelman, Gerald

publication date

  • 1978

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Limited digestion of the intact subunit of concanavalin A (Mr = 26,000) with trypsin followed by affinity chromatography on Sephadex G-100 has yielded a highly purified product designated here as Tn-Con A. Chemical studies have shown that Tn-Con A is composed of several components: a large fragment (Tn I, Mr = 19,000) spanning residues 1 to 172, and lower molecular weight polypeptides that are noncovalently associated with Tn I to form the active molecule. The molecular weight of Tn-Con A at pH 7 was 90,000, suggesting that, like native concanavalin A, it was a tetramer at physiological pH. Equilibrium dialysis experiments showed that Tn-Con A bound 1 molecule of alpha-methyl-D-glucoside/22,000 g atoms of protein and therefore that four saccharides are bound by the tetrameric molecule. Tn-Con A and native concanavalin A competed for the same receptors on the lymphocyte surface. Moreover, Tn-Con A was mitogenic for both mouse and human lymphocytes with dose-response curves similar to those of the native lectin. All of these results indicate that tryptic hydrolysis of concanavalin A produces a fragmented molecule retaining the saccharide-binding, subunit association, and mitogenic capacity of the native protein.

subject areas

  • Amino Acids
  • Animals
  • Biological Assay
  • Concanavalin A
  • Lymphocyte Activation
  • Methylglucosides
  • Methylglycosides
  • Mice
  • Molecular Weight
  • Pepsin A
  • Peptide Fragments
  • Protein Binding
  • Trypsin
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 346587
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Additional Document Info

start page

  • 3008

end page

  • 3015

volume

  • 253

issue

  • 9

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