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  • Author or Editor: Minoru Izumi x
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Equine α1-acid glycoprotein (α1 ag) was isolated from equine serum by successive ammonium precipitation, anion- and cation-exchange chromatographies, and gel filtration. Purified equine α1 ag had a molecular weight of 46,000 ± 1,000, and contained 31.4% carbohydrate. Gel isoelectric focusing revealed an isoelectric point range of 2.8 to 3.7. With immunoelectrophoresis, it was found that α1 ag migrated to the α1-globulin region.

Single radial immunodiffusion was used for quantitative measurement of α1 ag in equine serum. In clinically normal foals, serum α1 ag was undetectable (≤ 20 ng/ml) in ≤ 7-day-old foals, but was detected by 14 days. The α1 ag concentration (mean ± sd) increased to reach mean adult values of 99.23 ± 26.90 μg/ml by 1 year of age. The α1 ag concentration in pregnant mares decreased at 2 to 3 months before parturition, then gradually increased until 1 day after parturition, when a brief decrease was observed. The concentration increased again at 2 weeks after foaling, then a decrease was observed, after which the α1 ag concentration increased again by 2 to 4 months after parturition.

The concentration of serum α1 ag quickly rose to peak values 2 to 3 days after castration and jejunojejunostomy in adult horses, returning to baseline values by 14 to 28 days after surgery. The α1 ag was concluded to be an acute-phase reactive protein in horses.

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in American Journal of Veterinary Research