Rapid degradation of cucumber cotyledon lipoxygenase.

The lipoxygenase activity from cucumber cotyledons grown with their embryonic axis was separated into two fractions having M(r)s of 90,000 and 96,000, respectively, by hydrophobic chromatography. However, from de-embryonated cucumber cotyledons, only one form of lipoxygenase having a M(r) of 90,000 was purified. The three lipoxygenases could not be distinguished from each other either immunologically or by their enzymatic properties. Furthermore, peptide maps of the 90,000 and 96,000-lipoxygenases were identical. In a crude homogenate of cucumber cotyledons, the 96,000-lipoxygenase was rapidly degraded to the 90,000-form. Thus, it was inferred that the 90,000-lipoxygenase was probably the 96,000-form which had lost a peptide fragment of 6,000. It is suggested that there is a specific proteolytic activity for the degradation of 96,000-lipoxygenase. Estimation of changes in the proteolytic activity during seedling growth suggests that the activity at least partly contributes to the rapid in vivo degradation of cucumber cotyledon lipoxygenase.