鹿免疫球蛋白M和免疫球蛋白G的纯化与特性分析

The purification and characterisation of cervine IgM and IgG.

作者信息

Hibma M H, Griffin J F

机构信息

Microbiology Dept., University of Otago, Dunedin, New Zealand.

出版信息

Vet Immunol Immunopathol. 1990 Dec;26(4):343-52. doi: 10.1016/0165-2427(90)90118-c.

DOI:10.1016/0165-2427(90)90118-c

PMID:2075697

Abstract

A procedure is described for the isolation of immunoglobulin G (IgG) and immunoglobulin M (IgM) from hyperimmune cervine serum. Hybrids of red deer (Cervus elaphus) and wapiti (Cervus canadensis) were immunised with keyhole limpet hemocyanin (KLH). An immunoglobulin-containing fraction was precipitated from the hyperimmune serum using ammonium sulphate. The antigen-specific immunoglobulins were purified by KLH-conjugated sepharose affinity chromatography and further separated into IgM and IgG by gel-filtration chromatography. Purified immunoglobulin was analysed by polyacrylamide gel electrophoresis and isoelectric focusing. The molecular weights and isoelectric points of the composite chains of cervine IgG and IgM are presented.

摘要

本文描述了一种从超免疫鹿血清中分离免疫球蛋白G（IgG）和免疫球蛋白M（IgM）的方法。用钥孔戚血蓝蛋白（KLH）免疫马鹿（Cervus elaphus）和梅花鹿（Cervus canadensis）的杂交种。使用硫酸铵从超免疫血清中沉淀出含免疫球蛋白的部分。通过KLH偶联的琼脂糖亲和色谱法纯化抗原特异性免疫球蛋白，并通过凝胶过滤色谱法进一步分离为IgM和IgG。通过聚丙烯酰胺凝胶电泳和等电聚焦分析纯化的免疫球蛋白。给出了鹿IgG和IgM复合链的分子量和等电点。