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.

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Somatic embryogenesis of Cichorium intybus L. var. 'Carolus' is induced using cubical pieces of mature tap roots with an intervening callus phase. A Murashige and Skoog's (MS) semi solid basal medium supplemented with 2,4-dichlorophenoxyacetic acid (0.02 or 0.2 mg/l) and benzylaminopurine (0.25 mg/l) and a liquid MS medium devoid of growth regulators are used respectively for induction of callus and somatic embryoids and for further development and germination. Regeneration from the nodular proembryonal stage to the full grown embryoids occurs following different morphological pathways depending on the physical and chemical environment of the culture. Further development of these embryos into plantlets and the possibilities of application of this technique in plantbreeding have been discussed.