Purification and partial characterization of an extracellular melanoprotein from the fungus Venturia inaequalis

Show simple item record

dc.identifier.uri http://dx.doi.org/10.15488/2469
dc.identifier.uri http://www.repo.uni-hannover.de/handle/123456789/2495
dc.contributor.author Singh, P.
dc.contributor.author Piotrowski, M.
dc.contributor.author Gau, A.E.
dc.date.accessioned 2017-11-24T11:46:33Z
dc.date.available 2017-11-24T11:46:33Z
dc.date.issued 2005
dc.identifier.citation Singh, P.; Piotrowski, M.; Gau, A.E.: Purification and partial characterization of an extracellular melanoprotein from the fungus Venturia inaequalis. In: Zeitschrift für Naturforschung - Section C Journal of Biosciences 60 (2005), Nr. 1-2, S. 109-115. DOI: https://doi.org/10.1515/znc-2005-1-220
dc.description.abstract The fungus Venturia inaequalis clone No. 36 isolated from Malus domestica cv. Gloster excretes a melanoprotein of 36 kDa in relatively high amounts during growth in liquid culture. The protein was isolated from the culture medium and purified to homogeneity. It was shown to contain melanin. After raising an antiserum against the isolated protein, the protein could be shown to be located in the apoplast fluid of the V. inaequalis infected Malus domestica cv. Elstar. Partial sequencing of the protein revealed no significant sequence homologies to so far sequenced proteins. The melanoprotein binds ferrous and ferric iron. Moreover, it could be shown that the binding of ferric iron (but not of ferrous iron) leads to a change in the absorbance of the protein suggesting a modification of the protein by ferric, but not by ferrous, iron. In addition to iron, the protein also binds copper, but does not bind manganese or nickel. A possible function of this protein in the recruiting and transport of iron and copper and/or in the protection of the fungus by metal-ion mediated oxidative stress is discussed. © 2005 Verlag der Zeitschrift für Naturforschung. eng
dc.language.iso eng
dc.publisher Berlin : De Gruyter
dc.relation.ispartofseries Zeitschrift für Naturforschung - Section C Journal of Biosciences 60 (2005), Nr. 1-2
dc.rights CC BY-NC-ND 3.0
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/3.0/
dc.subject Apoplast eng
dc.subject Melanoprotein eng
dc.subject Venturia inaequalis eng
dc.subject fungal protein eng
dc.subject melanin eng
dc.subject melanoproteins eng
dc.subject metal eng
dc.subject peptide fragment eng
dc.subject protein eng
dc.subject amino acid sequence eng
dc.subject article eng
dc.subject Ascomycetes eng
dc.subject chemistry eng
dc.subject culture medium eng
dc.subject growth, development and aging eng
dc.subject isolation and purification eng
dc.subject kinetics eng
dc.subject metabolism eng
dc.subject molecular genetics eng
dc.subject molecular weight eng
dc.subject Amino Acid Sequence eng
dc.subject Ascomycota eng
dc.subject Culture Media eng
dc.subject Fungal Proteins eng
dc.subject Kinetics eng
dc.subject Melanins eng
dc.subject Metals eng
dc.subject Molecular Sequence Data eng
dc.subject Molecular Weight eng
dc.subject Peptide Fragments eng
dc.subject Proteins eng
dc.subject Fungi eng
dc.subject Malus x domestica eng
dc.subject Venturia inaequalis eng
dc.subject.ddc 570 | Biowissenschaften, Biologie ger
dc.title Purification and partial characterization of an extracellular melanoprotein from the fungus Venturia inaequalis
dc.type article
dc.type Text
dc.relation.essn 1865-7125
dc.relation.issn 0939-5075
dc.relation.doi https://doi.org/10.1515/znc-2005-1-220
dc.bibliographicCitation.issue 1-2
dc.bibliographicCitation.volume 60
dc.bibliographicCitation.firstPage 109
dc.bibliographicCitation.lastPage 115
dc.description.version publishedVersion
tib.accessRights frei zug�nglich


Files in this item

The following license files are associated with this item:

This item appears in the following Collection(s):

Show simple item record

 

Search the repository


Browse

My Account

Usage Statistics