Summary: The lectin in is a major protein, although its function was previously unknown. An enzyme-linked immunosorbent assay was developed to quantify the lectin content in mycelium, sclerotia and culture filtrate during the development of grown in a synthetic medium. Lectin content was low in young mycelium but increased dramatically at the onset of sclerotium formation, reaching a maximum in adult sclerotia. Upon myceliogenic germination, the lectin content of the sclerotia rapidly decreased. It thus appears that the lectin is a developmental regulated sclerotium-specific protein accumulating during sclerotium formation and disappearing during germination. Its relative abundance and the pattern of developmental control suggests that the lectin is probably a storage protein. Lectin accumulation was also influenced by the composition of the medium. Addition of supplementary carbohydrate (-glucose) caused a marked reduction in lectin content whereas increased nitrogen in the form of -asparagine led to a higher lectin content. However, when the -asparagine concentration was too high, autolysis occurred and part of the lectin was released into the medium.


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