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Mitsubishi Electric MXZ-18TV -E1 Service Manual page 39

Inverter-controlled multi system

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Antimicrobial activity of LTPs isolated from barley (Hordewn vulgare), maize
(Zea mays), spinach (Spitlacia olerucea), thale cress (Arabidopsis rholiuna), radish
(Rnphanus sativrrs), and broccoli (Bra.ssica nc~pus) (Molina and Garcia-Olmcdo,
1991; Thoma el 01.. 1994) have heen reported. The in virro antibiotic properties of
LTPs against various bacterial and fungal plant pathogens are well established
(Molina and Garcia-Olmedo. 1991; Terras et 01.. 1992; Molina et rrl., 1993; Segura er
01.. 1993). Their distribution at high concentrations over exposed surfaces, in vascular
tissue systems and Lrp-gene expression in response to infection by pathogens suggest
that they are active plant-defense proteins (Fleming et ul., 1992; Molina and Garcia-
Olmedo, 1993; Thoma er al., 1993; Pyee er ul., 1994). Garcia-Olmedo er ol., (1995)
reported the evidence supporting defensive role for ns-LTPs in plants. The relative
activities of different LTPs vary between pathogens, suggesting that they have some
degree of specificity. While certain LTPs were much more active than thionins
against the bacterial pathogen Clavibucrer michigunensis sub sp. sepedonicus, the
opposite was true against the fungus Fusurium solani, indicating that these families of
antimicrobial peptides might complement each other when simultaneously present in
a tissue (Molina et al., 1993; Garcia-Olmedo et al., 1995).
Antifungal protein purified from pearl millet seeds showed sequence
homology at the N-terminal sequence of the protein (25 residues) with the lipid
transfer proteins of cotton, wheat and barley. The purified protein had a molecular
mass of 25 kDa
and
showed an inhibitory effect
on
the mycelial growth Trichoderma
viridae and Rhizoctonia solani the rice sheath blight fungus in virro (Velazhahan et
al., 2001). An antifungal protein purified to homogeneity was characterized from
sunflower (Helianthus annuus
L.)
seeds (Ha-APlO) exerted
a
fungistatic effect that

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