AI Article Synopsis
- The study examines the acidic proteolytic activity in buckwheat seeds across different stages: developing, mature, and germinating, using various analytical techniques.
- Immunoblot analysis identified a specific proteolytic activity linked to a 47 kDa heterodimer composed of 31 kDa and 16 kDa subunits, suggesting its significance during seed maturation.
- The research also indicated that this proteinase exhibits milk-clotting activity and begins to accumulate 12 days after pollination, remaining present at the onset of germination.
Article Abstract
The pepstatin A sensitive acidic proteolytic activity of total protein extracts of buckwheat seeds has been analyzed in developing, mature, and germinating seeds by activity measurements as well as by electrophoretic and immunochemical techniques. Immunoblot analysis using cross-reactive antibodies raised against barley phytepsin suggested that specific proteolytic activity could be attributed to a 47 kDa heterodimeric polypeptide, composed of two subunits: 31 and 16 kDa polypeptides. The analysis of time course expression revealed that the 47 kDa heterodimer accumulated during seed maturation starting from 12 days after pollination and was also present at the beginning of germination. Milk-clotting activity of this proteinase was also indicated.
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| http://dx.doi.org/10.1021/jf026043b | DOI Listing |
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