Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10841179 | Plant Science | 2005 | 7 Pages |
Abstract
Leucine aminopeptidase (LAP) is a terminal enzyme catalyzing a cycle of protein turnover. The normal properties of LAP from plants show a hexameric structure, thermostability over 60 °C and optimum pH of approximately 9.5. We isolated three types of LAP from etiolated barley seedlings, which were designated as LAP 1, LAP 2 and LAP 3. All of the subunit compositions were 57 kDa of monomeric structure. The thermostability of LAP 1, LAP 2 and LAP 3 was indicated by the enzymes having 50% of maximum activities, 51, 54 and 56 °C, respectively. The optimum pH was 7.0 for LAP 1 and LAP 2, and 8.0 for LAP 3. LAP activity was found almost equally in leaf tissue, coleoptile and roots from etiolated and green seedlings. All LAPs were sensitive to p-chloromercuribenzoic acid. LAPs from barley seedlings provide novel properties compared to LAPs from other plant species.
Keywords
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Noriyuki Ogiwara, Toyoki Amano, Masashi Satoh, Yuzo Shioi,