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

The binding of purified, radioiodinated human C1q to baboon heart mitochondrial membranes was investigated. The interaction of C1q with heart mitochondrial membranes was shown to be readily saturable, specific for C1q, and reversible upon addition of unlabeled C1q or increasing salt concentrations....

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Bibliographic Details
Published in:The Journal of biological chemistry 1981-11, Vol.256 (21), p.10924-10929
Main Authors: Storrs, S B, Kolb, W P, Pinckard, R N, Olson, M S
Format: Article
Language:English
Subjects:
Animals
baboons
Binding, Competitive
Carrier Proteins
Complement Activating Enzymes - metabolism
Complement C1q
heart
Humans
Hyaluronan Receptors
Intracellular Membranes - metabolism
Kinetics
Membrane Glycoproteins
mitochondria
Mitochondria, Heart - metabolism
Mitochondrial Proteins
Osmolar Concentration
Papio
Protein Binding
Receptors, Complement - metabolism
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Summary:The binding of purified, radioiodinated human C1q to baboon heart mitochondrial membranes was investigated. The interaction of C1q with heart mitochondrial membranes was shown to be readily saturable, specific for C1q, and reversible upon addition of unlabeled C1q or increasing salt concentrations. Scatchard plots of the binding data were biphasic and yielded association constants on the order of 1 X 10(10) and 1 X 10(9) M-1 and binding capacities of approximately 0.16 and 0.24 nmol of C1q/mg of mitochondrial protein. The binding of C1q to isolated cardiac-derived mitochondrial membranes is implicated in the antibody-independent activation of the classical complement pathway by cellular membranes.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)68533-9