Journal of Lipid Research, Vol 26, 528-539, Copyright © 1985 by Lipid Research, Inc.
Monoclonal antibodies to rat C apolipoproteins: production and characterization of a unique antibody whose binding to apoC-I is inhibited by nonionic detergents
L Wong, PD Anderson, WR Gallaher and PS Roheim
Four monoclonal antibodies to rat apo (apolipoproteins) C were produced.
Three of the monoclonals reacted to apoC-I and one to apoC- III. The IgG
monoclonals LRB 21 and LRB 45 recognized a spatially close together or
identical apoC-I epitope. The monoclonal LRB 80, however, recognized an
epitope that is close to, but distinct from, that recognized by LRB 45 and
LRB 21. The antibody LRB 45 recognized an apoC- I epitope that is specific
for rat apoC-I, and the antibody did not cross-react with dog or human
lipoproteins. Rat apoC-I could be detected in all lipoprotein density
fractions, but not in the d greater than 1.21 g/ml fraction. Freezing and
thawing of serum did not alter the antibody antigen binding. However,
lipolysis of whole serum resulted in a 30% increase in antigenic epitope
expression. Antibody antigen reaction could be inhibited by subcritical
micellar concentration of nonionic detergents. The inhibition was specific
but could be partially reversed if lipid-containing serum was used as a
dilution buffer. On feeding animals a diet of olive oil and cholesterol for
2 weeks, apoC-I levels decreased.
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