Abstract
A double antibody radioimmunoassay (RIA) for rat apolipoprotein A-I is reported. The ApoA-I isolated from delipidated HDL by gel filtration yielded a single band on polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS), and its amino acid composition resembled that reported by others. ApoA-I was iodinated by lactoperoxidase and the resulting 125I-apoA-I was purified by gel filtration. Up to 93% of 125I-apoA-I was precipitable by antibody and greater than 99% of bound 125I-apoA-I was displaced by "cold" apoA-I. Other rat lopoproteins and apolipoproteins did not react in this system. Human plasma were also not reactive, nor were dog, goat, and sheep plasmas.
Highlights
A double antibody radioimmunoassay (RIA) for rat apolipoprotein A-I is reported
Since the rat is such a frequently used experimental species, we have developed a similar assay for rat apoA-I
I n RIA, speci$city is determined by the purityof the tracer [23]
Summary
A double antibody radioimmunoassay (RIA) for rat apolipoprotein A-I is reported. RatintactHDL displaced ‘251-apoA-I in parallel with “cold” apoA-I; only about 10% of the apoA-I i n intact HDL reacted in the assay. Removal of the lipid from HDL byextraction with ether-ethanol solutions increased the reactivity of apoA-I to levels expected from studies of the ape-4-I content of HDL by column chromatography and SDS disc gel electrophoresis. Plasmas from Sprague-Dawley male and female rats displaced counts in parallel with apoA-I. Lipid extraction increased apparent levels about 9-fold to 39 f 8 mg/dl for Sprague-Dawley males (n = 14) and 47 f 6 mg/dl for females (n = 5). Extraction of plasmas appears to be necessary to obtain accuralteevels of apoA-I in this assay system. This paper details the assay procedure, where it differs from ita counterpart for human apoA-I
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