Peumans W J, Smeets K, Van Nerum K, Van Leuven F, Van Damme E J
Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Heverlee, Belgium.
Planta. 1997;201(3):298-302. doi: 10.1007/s004250050070.
Analysis of nectar from leek (Allium porrum) flowers by SDS-PAGE revealed the presence of two major polypeptide bands of 50 kDa and 13 kDa, respectively. Using a combination of agglutination tests, enzyme assays and N-terminal sequencing, the polypeptides have been identified as subunits of alliin lyase (alliinase, EC 4.4.1.4) and mannose-binding lectin, respectively. The latter protein is particularly abundant since it represents about 75% of the total nectar protein. Honey produced by bees foraging on flowering leek plants still contains biologically active lectin and alliinase. However, the levels of both proteins are strongly reduced as compared to those in the original nectar. It is evident, therefore, that the lectin as well as the alliinase are inactivated/degraded during the conversion of nectar into honey.
通过SDS-PAGE对韭菜（葱属植物）花蜜进行分析，结果显示分别存在两条主要的多肽带，分子量分别为50 kDa和13 kDa。通过凝集试验、酶活性测定和N端测序相结合的方法，已将这些多肽分别鉴定为蒜氨酸裂解酶（蒜氨酸酶，EC 4.4.1.4）和甘露糖结合凝集素的亚基。后一种蛋白质特别丰富，因为它占花蜜总蛋白质的约75%。在开花的韭菜植物上觅食的蜜蜂所产蜂蜜中仍含有生物活性凝集素和蒜氨酸酶。然而，与原始花蜜中的蛋白质水平相比，这两种蛋白质的水平都大幅降低。因此，很明显，在花蜜转化为蜂蜜的过程中，凝集素和蒜氨酸酶都被灭活/降解了。
