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RESEARCH PRODUCT

Aspartic Proteinase from Barley Seeds is Related to Animal Cathepsin D

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In contrast to the well-characterized mammalian aspartic proteinases, plant aspartic proteinases have received little attention so far. Aspartic proteinase activity has been detected, for example, in resting seeds of scots pine (Salmia et al., 1978), soybean (Bond & Bowles, 1983), barley and wheat (Morris et al., 1985) as well as in leaves of orange (Garcia-Martinez & Moreno, 1986) and barley (Kervinen et al., 1990). Aspartic proteinases have been purified from the seeds of rice (Doi et al., 1980), cucumber, squash (Polanowski et al 1985) and wheat (Dunaevsky et al., 1989) as well as from the leaves of tomato (Rodrigo et al., 1989). The plant aspartic proteinases have been reported to enhance the hydrolysis of at least wheat (Belozersky et al., 1989) and cocoa (Heinrichs et al., 1990) storage proteins. Rodrigo et al (1989) have also suggested that the biological action of the pathogenesis related proteins in tomato leaves could be regulated by aspartic proteinases. Taken together, the specific functions of plant aspartic proteinases remain largely unknown.