Apolipoprotein A-I of primates.

Monkey apoA-I was isolated by ultracentrifugation or immunoprecipitation and analyzed by isoelectric focusing and two-dimensional polyacrylamide gel electrophoresis. The plasma apoA-I of 26 Old World monkeys (12 cynomolgus and 14 rhesus), 40 New World monkeys (8 cebus, 8 squirrel, 8 spider, 8 owl, and 8 marmosets), 6 prosimians (lemurs) and 10 apes (5 gibbons and 5 chimpanzees) were compared with each other as well as with human apoA-I. These analyses showed that monkey apoA-I contained one major and one to three minor (two basic and one acidic) isoproteins. The basic and acidic minor isoproteins differed by +2, +1, and -1 charges from the major apoA-I isoprotein designated apoA-I2. We have observed profound differences among the apoA-I electrophoretic patterns of the various primate species studied. The apparent isoelectric points of the major isoproteins of apoA-I of prosimians, Old World monkeys, New World monkeys, chimpanzees, gibbons, and humans were 5.70, 5.80, 5.35, 5.64, 5.42, and 5.64, respectively. The entire apoA-I isoprotein pattern of prosimians, Old World monkeys, chimpanzees, gibbons, and New World monkeys with respect to humans was shifted by approximately +1.5, +0.5, 0, -2.0, and -2.5 charges, respectively. The apoA-I synthesized by organ cultures of cynomolgus monkey intestine and liver overlaps on the two-dimensional system with the corresponding most basic minor plasma apoA-I isoprotein designated apoA-I2.(ABSTRACT TRUNCATED AT 250 WORDS)