ACTIVATORS AND INHIBITORS OF PROTEASE FROM COTYLEDONS OF CUCURBITA SEEDLINGS. | ||||
| Journal of Plant Production | ||||
| Article 12, Volume 1, Issue 4, April 2010, Page 633-644 PDF (484.59 K) | ||||
| Document Type: Original Article | ||||
| DOI: 10.21608/jpp.2010.86385 | ||||
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| Authors | ||||
| H. M. El-Shora; Hala S. Taha | ||||
| Mansoura University, Faculty of Scince, Botany Department, Egypt. | ||||
| Abstract | ||||
| Protease was isolated from cotyledons of 5-day old marrow (Cucurbita pepo L.) seedlings. The enzyme was induced by kinetin or benzyladenine (BA) at 50, 100 and 150 µmol. Protease was also induced by homobrassinolide (HBL) after treatment with 0.2, 0.4, 0.6, 0.8 or 1.0 µmol. Polyamines such as putrescine, spermine, cadaverine, spermidine and mixture of polyamines induced protease activity. Ca2+, K+ and Mg2+ activated protease activity when tested at either 5 or 10 mM. On the other hand, Co2+, Zn2+, Al3+, Cu2+ and Hg2+ inhibited the enzyme activity. AMP, ADP and ATP induced protease activity. Surfactants such as Triton X-100, Tween 60 and Tween 80 increased protease activity when added in the range of 0.2-1.2 % (v/v). Treatment with various concentrations of CdCl2 and PbCl2 resulted in inhibition of protease activity and PbCl2 was the stronger inhibitor. EDTA as chelating agent inhibited protease activity. | ||||
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