Bark lectins from the elderberry species belonging to the genus Sambucus have a unique carbohydrate binding specificity for sialylated glycoconjugates containing NeuAc(alpha 2-6)Gal/GalNAc sequence. To elucidate the structure of the elderberry lectin, a cDNA library was constructed from the mRNA
A type II ribosome-inactivating protein (RIP) was isolated from the bark tissue of Japanese elderberry (Sambucus sieboldiana) and named sieboldin-b. Sieboldin-b is a heterodimeric protein consisting of 27- and 33-kDa subunits and showed strong ribosome-inactivating activity in vitro but did not show
One of the ribosome inactivating proteins (RIPs), beta-momorcharin, and a lectin were isolated from seeds of the bitter melon Momordica charantia (Family Cucurbitaceae) in accordance with published procedures. Both beta-momorcharin and M. charantia lectin were then subjected to amino acid
BACKGROUND
Lactoferrin is an iron-binding protein belonging to the transferrin family. In addition to iron homeostasis, lactoferrin is also thought to have anti-microbial, anti-inflammatory, and anticancer activities. Previous studies showed that all lactoferrins are glycosylated in the human body,
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