SITE-SPECIFIC IMMOBILIZATION OF ANTIBODIES BY THEIR OLIGOSACCHARIDE MOIETIES TO NEW HYDRAZIDE DERIVATIZED SOLID SUPPORTS
SITE-SPECIFIC IMMOBILIZATION OF ANTIBODIES BY THEIR OLIGOSACCHARIDE MOIETIES TO NEW HYDRAZIDE DERIVATIZED SOLID SUPPORTS
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DOI：
10.1016/0022-1759(88)90041-5
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发表时间：
1988-08-09
影响因子：
2.2
通讯作者：
OSHANNESSY, DJ
中科院分区：
文献类型：
--
作者：
HOFFMAN, WL;OSHANNESSY, DJ
本报告描述了一种将抗体固定在固体载体上的新方法。抗体通过抗体碳水化合物侧链上生成的醛和固体载体上的肼基团之间的共价键结合到固体载体上。所形成的腙键至少在pH 2-10范围内是稳定的，允许抗原从亲和柱中被酸洗脱。每毫升固体载体中有超过25mg亲和纯化的兔IgG结合，大多数结合抗体保持生物活性。本文讨论了这种新的亲和支持相对于现有技术的优点，以及制备和使用含有单克隆或多克隆抗体的亲和柱的程序。
This report describes a new method for immobilization of antibodies to solid supports. Antibodies are bound to the solid supports by covalent bonds between aldehydes generated on the carbohydrate side chains of the antibody and hydrazide groups on the solid support. The hydrazone bonds that are formed are stable at least from pH 2-10, permitting the acid elution of antigens from the affinity column. Over 25 mg of affinity-purified rabbit IgG binds per ml of solid support, with most of the bound antibodies retaining biological activity. Advantages of this new affinity support over existing technology are discussed along with procedures for the preparation and use of affinity columns containing monoclonal or polyclonal antibodies.