کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10841179 | 1067884 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Leucine aminopeptidase from etiolated barley seedlings: characterization and partial purification of isoforms
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Plant Science - Volume 168, Issue 3, March 2005, Pages 575-581
Journal: Plant Science - Volume 168, Issue 3, March 2005, Pages 575-581
نویسندگان
Noriyuki Ogiwara, Toyoki Amano, Masashi Satoh, Yuzo Shioi,