caa a22 4500 477132707 CHVBK 20180405111708.0 cr unu---uuuuu 170330e19970601xx s 000 0 eng 10.1023/A:1018323021721 doi (NATIONALLICENCE)springer-10.1023/A:1018323021721 Immunological characterization of a 36 kDa Fe deficiency specific peptide in barley roots [Elektronische Daten] [Koichiro Suzuki, Kenji Kanazawa, Kyoko Higuchi, Naoko Nishizawa, Satoshi Mori] In a previous paper we reported that an acidic 36 kDa peptide is the most strongly induced peptide among several peptides induced by Fe deficiency in barley roots. In this paper, polyclonal antibodies were raised against the 36 kDa peptide. This peptide appeared in the roots of all the graminaceous species tested (barley, rye, wheat, oat, maize, sorghum and rice) in response to Fe deficiency. More of the peptide was found in the roots of graminaceous species which secrete higher amounts of mugineic acids (MAs) under Fe deficient nutrition status. Induction of the 36 kDa peptide was first observed on the third day of Fe deficiency, rising to a maximum value on the seventh day. The trend has a positive correlation with secretion of MAs during Fe deficiency. Further, resupply of Fe resulted in a decrease in peptide production on the second day, reaching a control level on the seventh day. The rate of decrease in peptide production was observed to be slower than that of MA secretion. Other nutrient stresses such as B excess, B deficiency, Cu excess, Cu deficiency, Mn excess, Mn deficiency, Zn excess and Zn deficiency induced far less of the peptide. The specific expression of the 36 kDa peptide in roots of graminaceous species under Fe deficiency suggested the positive association of the peptide with a specific Fe deficiency tolerance mechanism in graminaceous plants. Chapman and Hall, 1997 barley roots nationallicence graminaceous plants nationallicence immunoblotting nationallicence iron deficiency nationallicence 36 kDa peptide nationallicence 2D-PAGE nationallicence Suzuki Koichiro Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut Kanazawa Kenji Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut Higuchi Kyoko Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut Nishizawa Naoko Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut Mori Satoshi Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut Biometals Kluwer Academic Publishers 10/2(1997-06-01), 77-84 0966-0844 10:2<77 1997 10 10534 https://doi.org/10.1023/A:1018323021721 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018323021721 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Suzuki Koichiro Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut NATIONALLICENCE 700 1- Kanazawa Kenji Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut NATIONALLICENCE 700 1- Higuchi Kyoko Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut NATIONALLICENCE 700 1- Nishizawa Naoko Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut NATIONALLICENCE 700 1- Mori Satoshi Laboratory of Plant Molecular Physiology, The University of Tokyo, Tokyo, Japan aut NATIONALLICENCE 773 0- Biometals Kluwer Academic Publishers 10/2(1997-06-01), 77-84 0966-0844 10:2<77 1997 10 10534 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer