Isolation of the Third Component of Complement (C3) from Carp Serum

Miki Nakao, Tomoki Yano, Hiroko Matsuyama, Takeshi Uemura

研究成果: ジャーナルへの寄稿記事

20 引用 (Scopus)

抄録

The third component (C3) of carp complement was purified to homogeneity by a four-step purification procedure: 1) affinity chromatography on Blue-Cellulofine, 2) QAE-Sephadex A-50 chromatography, 3) gel filtration on Sepharose CL-6B, and 4) CM-Sephadex C-50 chromatography. Hemolytic activity of carp C3 was assayed using intermediate cells, EAC14, and hydrazine-treated carp serum. The final recovery of C3 activity was 17%. Carp C3 showed an electrophoretic mobility of B-globulin with a molecular weight of 194,000. The protein consisted of two carbohydrate-containing subunits of 120,000 (a-chain) and 74,000 (B-chain) which were linked by disulfide bonds. In agreement with mammalian C3, carp C3 was inactivated by nucleophilic attack by amines such as hydrazine, ammonia, hydroxylamine and methylamine, but it showed considerable resistance against chaotropic reagents such as KBr and KSCN. In addition, it was shown that carp C3 attached covalently to a zymosan particle as a result of the activation of the alternative complement pathway.

元の言語英語
ページ(範囲)2021-2027
ページ数7
ジャーナルNIPPON SUISAN GAKKAISHI
55
発行部数11
DOI
出版物ステータス出版済み - 1 1 1989

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carp
chromatography
serum
complement
hydrazine
homogeneity
purification
carbohydrate
ammonia
gel
methylamine
zymosan
protein
disulfide bonds
affinity chromatography
amines
globulins
agarose
gels
molecular weight

All Science Journal Classification (ASJC) codes

  • Aquatic Science

これを引用

Isolation of the Third Component of Complement (C3) from Carp Serum. / Nakao, Miki; Yano, Tomoki; Matsuyama, Hiroko; Uemura, Takeshi.

:: NIPPON SUISAN GAKKAISHI, 巻 55, 番号 11, 01.01.1989, p. 2021-2027.

研究成果: ジャーナルへの寄稿記事

Nakao, Miki ; Yano, Tomoki ; Matsuyama, Hiroko ; Uemura, Takeshi. / Isolation of the Third Component of Complement (C3) from Carp Serum. :: NIPPON SUISAN GAKKAISHI. 1989 ; 巻 55, 番号 11. pp. 2021-2027.
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abstract = "The third component (C3) of carp complement was purified to homogeneity by a four-step purification procedure: 1) affinity chromatography on Blue-Cellulofine, 2) QAE-Sephadex A-50 chromatography, 3) gel filtration on Sepharose CL-6B, and 4) CM-Sephadex C-50 chromatography. Hemolytic activity of carp C3 was assayed using intermediate cells, EAC14, and hydrazine-treated carp serum. The final recovery of C3 activity was 17{\%}. Carp C3 showed an electrophoretic mobility of B-globulin with a molecular weight of 194,000. The protein consisted of two carbohydrate-containing subunits of 120,000 (a-chain) and 74,000 (B-chain) which were linked by disulfide bonds. In agreement with mammalian C3, carp C3 was inactivated by nucleophilic attack by amines such as hydrazine, ammonia, hydroxylamine and methylamine, but it showed considerable resistance against chaotropic reagents such as KBr and KSCN. In addition, it was shown that carp C3 attached covalently to a zymosan particle as a result of the activation of the alternative complement pathway.",
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N2 - The third component (C3) of carp complement was purified to homogeneity by a four-step purification procedure: 1) affinity chromatography on Blue-Cellulofine, 2) QAE-Sephadex A-50 chromatography, 3) gel filtration on Sepharose CL-6B, and 4) CM-Sephadex C-50 chromatography. Hemolytic activity of carp C3 was assayed using intermediate cells, EAC14, and hydrazine-treated carp serum. The final recovery of C3 activity was 17%. Carp C3 showed an electrophoretic mobility of B-globulin with a molecular weight of 194,000. The protein consisted of two carbohydrate-containing subunits of 120,000 (a-chain) and 74,000 (B-chain) which were linked by disulfide bonds. In agreement with mammalian C3, carp C3 was inactivated by nucleophilic attack by amines such as hydrazine, ammonia, hydroxylamine and methylamine, but it showed considerable resistance against chaotropic reagents such as KBr and KSCN. In addition, it was shown that carp C3 attached covalently to a zymosan particle as a result of the activation of the alternative complement pathway.

AB - The third component (C3) of carp complement was purified to homogeneity by a four-step purification procedure: 1) affinity chromatography on Blue-Cellulofine, 2) QAE-Sephadex A-50 chromatography, 3) gel filtration on Sepharose CL-6B, and 4) CM-Sephadex C-50 chromatography. Hemolytic activity of carp C3 was assayed using intermediate cells, EAC14, and hydrazine-treated carp serum. The final recovery of C3 activity was 17%. Carp C3 showed an electrophoretic mobility of B-globulin with a molecular weight of 194,000. The protein consisted of two carbohydrate-containing subunits of 120,000 (a-chain) and 74,000 (B-chain) which were linked by disulfide bonds. In agreement with mammalian C3, carp C3 was inactivated by nucleophilic attack by amines such as hydrazine, ammonia, hydroxylamine and methylamine, but it showed considerable resistance against chaotropic reagents such as KBr and KSCN. In addition, it was shown that carp C3 attached covalently to a zymosan particle as a result of the activation of the alternative complement pathway.

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