Characterization of the binding of purified human C1q to heart mitochondrial membranes

S. B. Storrs, W. P. Kolb, R. N. Pinckard, M. S. Olson

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

The binding of purified, radioiodinated human Clq to baboon heart mitochondrial membranes was investigated. The interaction of Clq with heart mitochondrial membranes was shown to be readily saturable, specific for Clq, and reversible upon addition of unlabeled Clq or increasing salt concentrations Scatchard plots of the binding data were biphasic and yielded association constants on the order of 1 x 1010 and 1 x 109 M-1 and binding capacities of approximately 0.16 and 0.24 nmol of Clq/mg of mitochondrial protein. The binding of Clq to isolated cardiac-derived mitochondrial membranes is implicated in the antibody-independent activation of the classical complement pathway by cellular membranes.

Original languageEnglish (US)
Pages (from-to)10924-10929
Number of pages6
JournalJournal of Biological Chemistry
Volume256
Issue number21
StatePublished - Dec 1 1981

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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