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Large-scale purification of choline acetyltransferase and production of highly specific antisera.

作者信息

Ostermann C, Dickmann U, Muley T, Mäder M

机构信息

Neurologische Klinik und Poliklinik der Universität, Göttingen, Federal Republic of Germany.

出版信息

Eur J Biochem. 1990 Aug 28;192(1):215-8. doi: 10.1111/j.1432-1033.1990.tb19217.x.

DOI:10.1111/j.1432-1033.1990.tb19217.x
PMID:2401292
Abstract

Choline acetyltransferase (ChAT) was purified by immunoaffinity chromatography using a covalently immobilized monoclonal antibody. In a two-step procedure, 10 kg porcine brain yielded 750 micrograms active enzyme of apparent homogeneity. This amount of ChAT was purified routinely. The purification factor was 18,000 and the yield of activity 4.3%. The affinity resin was stable under the experimental conditions applied and was used many times. The highly purified enzyme was subsequently employed to obtain a specific anti-ChAT antiserum of high titer.

摘要

相似文献

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Large-scale purification of choline acetyltransferase and production of highly specific antisera.
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