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牛α-乳白蛋白和β-乳球蛋白之间存在共同表位的证据。

Evidence for a common epitope between bovine alpha-lactalbumin and beta-lactoglobulin.

作者信息

Baroglio C, Giuffrida M G, Cantisani A, Napolitano L, Bertino E, Fabris C, Conti A

机构信息

Centro Studi Alimentazione Animali, CNR, Torino, Italy.

出版信息

Biol Chem. 1998 Dec;379(12):1453-6.

PMID:9894814
Abstract

The aim of this work was to check and quantify any cross-reactivities among the main bovine whey proteins, utilizing purified polyclonal antibodies against bovine beta-lactoglobulin, alpha-lactalbumin and serum albumin, and to identify possible common epitope(s). Purified polyclonal anti-bovine beta-lactoglobulin antibodies show 10% cross-reactivity with bovine alpha-lactalbumin, both in its native and its denatured form. A continuous stretch of four amino acids common to alpha-lactalbumin and beta-lactoglobulin that might be responsible for this cross-reactivity has been identified. Cross-reactivity between this antibody and bovine serum albumin is, on the contrary, negligible. Purified polyclonal anti-bovine alpha-lactalbumin and anti-serum albumin antibodies do not cross-react.

摘要

这项工作的目的是利用针对牛β-乳球蛋白、α-乳白蛋白和血清白蛋白的纯化多克隆抗体,检测并量化主要牛乳清蛋白之间的任何交叉反应,并确定可能的共同表位。纯化的多克隆抗牛β-乳球蛋白抗体在天然和变性形式下均与牛α-乳白蛋白表现出10%的交叉反应。已鉴定出α-乳白蛋白和β-乳球蛋白共有的一段连续四个氨基酸,这可能是导致这种交叉反应的原因。相反,该抗体与牛血清白蛋白之间的交叉反应可忽略不计。纯化的多克隆抗牛α-乳白蛋白抗体和抗血清白蛋白抗体不发生交叉反应。

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