| Autor: |
Frostell, Å., Mendel-Hartvig, I., Nelson, B. D., Tötterman, T. H., Björkland, A., Ragan, I. C., Cleeter, M. W. J., Patel, S. D. |
| Předmět: |
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| Zdroj: |
Scandinavian Journal of Immunology; Dec1988, Vol. 28 Issue 6, p645-652, 8p |
| Abstrakt: |
Anti-mitochondrial autoantibodics (AMA) from patients with primary biliary cirrhosis (PBC) were analysed for fine specificity by immunoblotting and enzyme-linked immunosorbent assay (ELISA). Inhibition ELISA showed that complex l (NADH-ubiquinone reductase) from beef heart mitochondria completely inhibited the binding of AMA to mitochondrial inner membranes (SMP), indicating that the major mitochondrial antigens are located in complex l. Immunoblot analysis of beef heart SMP, complex 1 and the iron sulphur (IP) subtraction of complex l revealed several antigens, one of which (75 kDa) reacted with all PBC sera but not with the additional autoimmune sera tested. Resolution of SMP or complex 1 by two-dimensional electrophoresis yielded in both preparations a polypeptide of 75 kDa with an isoelectric point of 6.4, which reacted with PBC serum and with rabbit antisera raised against the 75,000 subunit of complex 1. In immunoblot experiments, the antigenicity of the 75,000 polypeptide in SMP, complex I, and the IP subtraction is increased by prior reduction of the sample with mercaptoethanol. This suggests a similarity to the PBC-specific 'M-2' antigen, which is also sensitive to sulphur reagents. The data indicate that the 75 kDa polypeptide of complex I is a major mitochondrial antigen binding AMA in PBC sera, and allows us to identify the location and probable function of the PBC antigen. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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