Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Binding of alpha(2)-macroglobulin and limulin: Regulation of the plasma haemolytic system of the american horseshoe crab, limulus

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

Overview

authors

  • Swarnakar, S.
  • Asokan, P.
  • Quigley, James
  • Armstrong, P. B.

publication date

  • May 2000

journal

  • Biochemical Journal  Journal

abstract

  • The mediator of haemolysis in the plasma of the horseshoe crab, Limulus polyphemus, is limulin, a sialic acid-binding lectin. The haemolytic activity of limulin is inhibited by thiol ester-reacted forms of Limulus alpha(2)-macroglobulin, the third-most abundant protein of the plasma. Limulus alpha(2)-macroglobulin that has experienced cleavage of its internal thiol ester bond, consequent to reaction with proteases, or with the small primary amine, methylamine, reduces the haemolytic activity of limulin when present at molar excesses that approximate the relative concentrations of these two proteins in the plasma. Native, unreacted Limulus alpha(2)-macroglobulin has no effect on the haemolytic activity of limulin. Limulin binds thiol ester-reacted forms of Limulus alpha(2)-macroglobulin both in a solid-phase assay and in solution with an avidity 10-25 times higher than native, unreacted Limulus alpha(2)-macroglobulin. Protease-reacted alpha(2)-macroglobulin functions as a marker for the presence of foreign proteases in the blood of Limulus, and thus of pathogenic organisms that release proteases as facilitators of invasion and pathogenicity. Modulation of the haemolytic system represents a novel function for alpha(2)-macroglobulin.

subject areas

  • Animals
  • Biotinylation
  • Calcium
  • Dextrans
  • Endopeptidases
  • Hemagglutinins
  • Hemolysis
  • Horseshoe Crabs
  • Lectins
  • Ligands
  • Methylamines
  • Molecular Weight
  • Osmolar Concentration
  • Protein Binding
  • Sodium Chloride
  • Solutions
  • Sulfhydryl Compounds
  • alpha-Macroglobulins
scroll to property group menus

Research

keywords

  • cytolysis
  • innate immunity
  • lectin
  • pentraxin
  • proteinase clearance
  • thiol ester
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0264-6021

Digital Object Identifier (DOI)

  • 10.1042/0264-6021:3470679

PubMed ID

  • 10769170
scroll to property group menus

Additional Document Info

start page

  • 679

end page

  • 685

volume

  • 347

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support