LECTIN AND ALLIINASE ARE THE PREDOMINANT PROTEINS IN NECTAR FROM LEEK(ALLIUM-PORRUM L.) FLOWERS

Citation
Wj. Peumans et al., LECTIN AND ALLIINASE ARE THE PREDOMINANT PROTEINS IN NECTAR FROM LEEK(ALLIUM-PORRUM L.) FLOWERS, Planta, 201(3), 1997, pp. 298-302
Citations number
26
Categorie Soggetti
Plant Sciences
Journal title
PlantaACNP
ISSN journal
00320935
Volume
201
Issue
3
Year of publication
1997
Pages
298 - 302
Database
ISI
SICI code
0032-0935(1997)201:3<298:LAAATP>2.0.ZU;2-N
Abstract
Analysis of nectar from leek (allium porrum) flowers by SDS-PAGE revea led the presence of two major polypeptide bands of 50 kDa and 13 kDa, respectively. Using a combination of agglutination tests, enzyme assay s and N-terminal sequencing, the polypeptides have been identified as subunits of alliin lyase (alliinase, EC 4.4.1.4) and mannose-binding l ectin, respectively. The latter protein is particularly abundant since it represents about 75% of the total nectar protein. Honey produced b y bees foraging on flowering leek plants still contains biologically a ctive lectin and alliinase. However, the levels df both proteins are s trongly reduced as compared to those in the original nectar. It is evi dent, therefore, that the lectin as well as the alliinase are inactiva ted/degraded during the conversion of nectar into honey.