ISOLATION AND CHARACTERIZATION OF BANLEC-I, A MANNOSIDE-BINDING LECTIN FROM MUSA-PARADISIAC (BANANA)
ISOLATION AND CHARACTERIZATION OF BANLEC-I, A MANNOSIDE-BINDING LECTIN FROM MUSA-PARADISIAC (BANANA)
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DOI：
10.1042/bj2720721
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发表时间：
1990-12-15
影响因子：
4.1
通讯作者：
AALBERSE, RC
中科院分区：
文献类型：
--
作者：
KOSHTE, VL;VANDIJK, W;AALBERSE, RC
从香蕉（Musa paradisiac）中分离出一种具有结合特异性的banleci凝集素（banleci），该凝集素对（Man）6GlcNAc以上大小级别的寡糖寡糖聚糖具有结合特异性。它不能凝集未经处理的人或羊红细胞，但能凝集兔红细胞。banleci刺激t细胞增殖。在尺寸排除色谱法上，banleci的分子质量约为。27 kDa，在SDS/PAGE上分子质量约为。13 kDa。等电点为7.2-7.5。banleci被发现是一种非常有效的检测糖蛋白的探针，例如在硝化纤维素印迹上。
A lectin (BanLec-I) from banana (Musa paradisiac) with a binding specificity for oligomannosidic glycans of size classes higher than (Man)6GlcNAc was isolated and purified by affinity chromatography on a Sephadex G-75 column. It did not agglutinate untreated human or sheep erythrocytes, but it did agglutinate rabbit erythrocytes. BanLec-I stimulated T-cell proliferation. On size-exclusion chromatography, BanLec-I has a molecular mass of approx. 27 kDa, and on SDS/PAGE the molecular mass is approx. 13 kDa. The isoelectric point is 7.2-7.5. BanLec-I was found to be very effective as a probe in detecting glycoproteins, e.g. on nitrocellulose blots.