Dirk K. Hincha
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Dirk K. Hincha has a total of 8 co-authors. Here are the top co-authors by number of shared publications:
Birgit Neukamm
Institut für Pflanzenphysiologie und Mikrobiologie, Freie Universität, Königin Luise-Strasse 12–16, D–14195 Berlin, Germany (D.K.H., B.N., H.A.M.S., F.S., W.W., J.M.S.);
1 shared publication- Frank Sieg
CuroNZ, 173 Cames Road, Mangawhai 0975, New Zealand
1 shared publication Hany A.M. Sror
Institut für Pflanzenphysiologie und Mikrobiologie, Freie Universität, Königin Luise-Strasse 12–16, D–14195 Berlin, Germany (D.K.H., B.N., H.A.M.S., F.S., W.W., J.M.S.);
1 shared publicationJürgen M. Schmitt
Institut für Pflanzenphysiologie und Mikrobiologie, Freie Universität, Königin Luise-Strasse 12–16, D–14195 Berlin, Germany (D.K.H., B.N., H.A.M.S., F.S., W.W., J.M.S.);
1 shared publicationMarkus Rückels
Boehringer Mannheim GmbH, Abteilung BP–Z 6, Division Biochemica, Nonnenwald 2, D–82372 Penzberg, Germany (M.R.);
1 shared publication- Valérie Lullien-Pellerin
INRA
1 shared publication
Latest Publications
- 1 February 2001
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 125 (2) , 835-846
Cabbage Cryoprotectin Is a Member of the Nonspecific Plant Lipid Transfer Protein Gene Family
We have recently purified a protein (cryoprotectin) from the leaves of cold-acclimated cabbage (Brassica oleracea) to electrophoretic homogeneity, which protects thylakoids isolated from the leaves of nonacclimated spinach (Spinacia oleracea) from freeze-thaw damage. Sequencing of cryoprotectin showed the presence of at least three isoforms of WAX9 proteins, which belong to the class of nonspecific lipid transfer proteins. Antibodies raised against two synthetic peptides derived from the WAX9 proteins recognized a band of approximately 10 kD in western blots of crude cryoprotectin preparations. This protein and the cryoprotective activity could be precipitated from solution by the antiserum. We show further that cryoprotectin is structurally and functionally different from WAX9 isolated from the surface wax of cabbage leaves. WAX9 has lipid transfer activity for phosphatidylcholine, but no cryoprotective activity. Cryoprotectin, on the other hand, has cryoprotective, but no lipid transfer activity. The cryoprotective activity of cryoprotectin was strictly dependent on Ca2+ and Mn2+ and could be inhibited by chelating agents, whereas the lipid transfer activity of WAX9 was higher in the presence of ethylenediaminetetraacetate than in the presence of Ca2+and Mn2+.
- 1 February 2001
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 125 (2) , 835-846
Cabbage Cryoprotectin Is a Member of the Nonspecific Plant Lipid Transfer Protein Gene Family
We have recently purified a protein (cryoprotectin) from the leaves of cold-acclimated cabbage (Brassica oleracea) to electrophoretic homogeneity, which protects thylakoids isolated from the leaves of nonacclimated spinach (Spinacia oleracea) from freeze-thaw damage. Sequencing of cryoprotectin showed the presence of at least three isoforms of WAX9 proteins, which belong to the class of nonspecific lipid transfer proteins. Antibodies raised against two synthetic peptides derived from the WAX9 proteins recognized a band of approximately 10 kD in western blots of crude cryoprotectin preparations. This protein and the cryoprotective activity could be precipitated from solution by the antiserum. We show further that cryoprotectin is structurally and functionally different from WAX9 isolated from the surface wax of cabbage leaves. WAX9 has lipid transfer activity for phosphatidylcholine, but no cryoprotective activity. Cryoprotectin, on the other hand, has cryoprotective, but no lipid transfer activity. The cryoprotective activity of cryoprotectin was strictly dependent on Ca2+ and Mn2+ and could be inhibited by chelating agents, whereas the lipid transfer activity of WAX9 was higher in the presence of ethylenediaminetetraacetate than in the presence of Ca2+and Mn2+.