Measurement of apolipoprotein A-I in rat high density lipoprotein and in rat plasma by radioimmunoassay.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005260:Female; D007457:Iodine Radioisotopes; D008075:Lipoproteins, HDL / Q000097:blood* / Q000276:immunology; D008297:Male; D008722:Methods; D011863:Radioimmunoassay; D051381:Rats / Q000097:blood*
D000596:Amino Acids; D007457:Iodine Radioisotopes; D008075:Lipoproteins, HDL