Journal
SCIENTIA HORTICULTURAE
Volume 164, Issue -, Pages 160-164Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.scienta.2013.09.005
Keywords
Japanese pear; RNase activity; Fruit set; Self-incompatibility; Metal salt
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [22380022]
- Grants-in-Aid for Scientific Research [22380022] Funding Source: KAKEN
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When inhibitory effects on stylar RNase activity were investigated in the Japanese pear (Pyrus pyrifolia Nakai), CuSO4 and ZnSO4 were significantly effective, and the inhibition was dose-dependent. Since MgSO4 and CaCl2 did not show any inhibition, the active ions would be Cu2+ and Zn2+. Because Cu2+ separated clearly from the stylar proteins when protein-CuSO4 mixture was loaded on Sephadex G-10 column chromatography, the cation may not be combined strongly with the protein. The RNase activity of the protein, furthermore, was almost completely recovered when the proteins were isolated from the mixture by (NH4)2SO(4) precipitation. Copper ions strongly reduced the RNase A activity, moderately RNase S and weakly RNase T-1 at 1 mM, while it did not affect the RNase B. The CuSO4 application at 2 mM induced more than 30% fruit set following self-pollination but Na2SO4 and K2SO4 did not, suggests that Cu2+ causes fruit set through reducing stylar RNase activity. (C) 2013 Elsevier B.V. All rights reserved.
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