Isolation and characterization of α1-acid glycoprotein from horses, and its evaluation as an acute-phase reactive protein in horses

Tomoko Taira From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Toru Fujinaga From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Keiji Tamura From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Minoru Izumi From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Hiroshi Itoh From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Nobuo Tsunoda From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Kazuto Yamashita From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Masahiro Okumura From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Shinya Mizuno From the Department of Veterinary Surgery, Faculty of Veterinary Medicine, Hokkaido University, Sapporo 060, Japan (Taira, Fujinage, Yamashita, Okumura, Mizuno), Saikinkagaku Institute, Sendai 981, Japan (Tamura, Izumi), Morioka Livestock Hygiene Service Center, Iwate 020-01, Japan (Itoh), and Shadai Farm, 275 Genbu, Hayakita-cho 059-14, Japan (Tsunoda).

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Summary

Equine α1-acid glycoprotein (α1ag) was isolated from equine serum by successive ammonium precipitation, anion- and cation-exchange chromatographies, and gel filtration. Purified equine α1ag 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 α1ag migrated to the α1-globulin region.

Single radial immunodiffusion was used for quantitative measurement of α1ag in equine serum. In clinically normal foals, serum α1ag was undetectable (≤ 20 ng/ml) in ≤ 7-day-old foals, but was detected by 14 days. The α1ag concentration (mean ± sd) increased to reach mean adult values of 99.23 ± 26.90 μg/ml by 1 year of age. The α1ag 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 α1ag concentration increased again by 2 to 4 months after parturition.

The concentration of serum α1ag 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 α1ag was concluded to be an acute-phase reactive protein in horses.

Summary

Equine α1-acid glycoprotein (α1ag) was isolated from equine serum by successive ammonium precipitation, anion- and cation-exchange chromatographies, and gel filtration. Purified equine α1ag 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 α1ag migrated to the α1-globulin region.

Single radial immunodiffusion was used for quantitative measurement of α1ag in equine serum. In clinically normal foals, serum α1ag was undetectable (≤ 20 ng/ml) in ≤ 7-day-old foals, but was detected by 14 days. The α1ag concentration (mean ± sd) increased to reach mean adult values of 99.23 ± 26.90 μg/ml by 1 year of age. The α1ag 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 α1ag concentration increased again by 2 to 4 months after parturition.

The concentration of serum α1ag 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 α1ag was concluded to be an acute-phase reactive protein in horses.

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