K
Karen G. Welinder
Researcher at Aalborg University
Publications - 115
Citations - 6809
Karen G. Welinder is an academic researcher from Aalborg University. The author has contributed to research in topics: Peroxidase & Horseradish peroxidase. The author has an hindex of 43, co-authored 114 publications receiving 6609 citations. Previous affiliations of Karen G. Welinder include University of Copenhagen & University of Birmingham.
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Journal ArticleDOI
Superfamily of plant, fungal and bacterial peroxidases
TL;DR: New peroxidase structures have significantly increased the understanding of the evolutionary and functional relationships within the plant per oxidase superfamily.
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Amino Acid Sequence Studies of Horseradish Peroxidase
TL;DR: Isoelectric points and charge distribution within the native protein, the apoprotein and the cyanogen bromide fragments, a buried pyrrolidonecarboxylyl amino terminus, heterogeneity at the carboxyl terminus are discussed, and a possible domain structure, likely from partial tryptic digestion is discussed.
Journal ArticleDOI
Structural diversity and transcription of class III peroxidases from Arabidopsis thaliana
Karen G. Welinder,Karen G. Welinder,Annemarie F. Justesen,Inger V. H. Kjærsgård,Rikke Beck Jensen,Søren K. Rasmussen,Hans M. Jespersen,Laurent Duroux +7 more
TL;DR: In this paper, the authors sequenced expressed sequence tags (ESTs) encoding novel heme-containing class III peroxidases from Arabidopsis thaliana and annotated 73 full-length genes identified in the genome.
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Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA
Jørgen Olsen,G M Cowell,Elaine Kønigshøfer,E. Michael Danielsen,Jette Møller,Liselotte Laustsen,Ole C. Hansen,Karen G. Welinder,Jan Engberg,Walter Hunziker,Martin Spiesst,Hans Sjöström,Ove Norén +12 more
TL;DR: The complete primary structure (967 amino acids) of an intestinal human aminopeptidase N was deduced from the sequence of a cDNA clone suggesting that the juxta‐ and intra‐membraneous parts of the molecule have been added/preserved during development.
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Purification and characterization of peroxidases correlated with lignification in poplar xylem
TL;DR: Two of the five isolated peroxidases found in the xylem of poplar could oxidize the lignin monomer analog syringaldazine, an activity previously correlated with lignification in poplar, and are suggested to be involved in lignIn polymerization.