大鼠肺中β-半乳糖苷结合蛋白的亚细胞定位。
The subcellular localization of the beta-galactoside-binding protein of rat lung.
作者信息
Sanford G L, Davis L D, Powell J T
出版信息
Biochem J. 1982 Apr 15;204(1):97-102. doi: 10.1042/bj2040097.
The subcellular localization of the beta-galactoside-binding protein, or lectin, from rat lung was investigated by the specific binding of anti-lectin immunoglobulin G to subcellular fractions. We used both adult and immature (12-day-old) rats; the immature rat lungs have an 8-10-fold greater concentration than adult rat lungs [Powell & Whitney (1980) Biochem. J. 188, 1-8]. In both groups of animals we observed greater specific binding of anti-lectin immunoglobulin G to intracellular membrane (mitochondrial and microsomal fractions) than to plasma membranes. Pre-incubation of membrane fractions with lactose resulted in a marked diminution of anti-lectin immunoglobulin G binding. In the adult rat lung most (approx. 80%) of the lectin activity was membrane-associated. In the immature rat lung only approx. 30% of the lectin activity was membrane associated and most of the beta-galactoside-binding protein appeared to be a soluble cytoplasmic component. The rat lung beta-galactoside-binding protein appeared to have a broad but predominantly intracellular location, being associated with membranes through one of its galactoside-binding sites.
通过抗凝集素免疫球蛋白G与亚细胞组分的特异性结合，研究了来自大鼠肺的β-半乳糖苷结合蛋白（即凝集素）的亚细胞定位。我们使用了成年大鼠和未成熟（12日龄）大鼠；未成熟大鼠肺中的凝集素浓度比成年大鼠肺高8 - 10倍[鲍威尔和惠特尼（1980年），《生物化学杂志》188卷，第1 - 8页]。在两组动物中，我们都观察到抗凝集素免疫球蛋白G与细胞内膜（线粒体和微粒体组分）的特异性结合比与质膜的结合更强。用乳糖对膜组分进行预孵育导致抗凝集素免疫球蛋白G结合显著减少。在成年大鼠肺中，大部分（约80%）的凝集素活性与膜相关。在未成熟大鼠肺中，只有约30%的凝集素活性与膜相关，并且大部分β-半乳糖苷结合蛋白似乎是一种可溶性细胞质成分。大鼠肺β-半乳糖苷结合蛋白似乎具有广泛但主要位于细胞内的定位，通过其一个半乳糖苷结合位点与膜相关。
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