TY  - JOUR
A1  - Cederkvist, F. Henning
A1  - Zamfir, Alina D.
A1  - Bahrke, Sven
A1  - Eijsink, Vincent G. H.
A1  - Sorlie, Morten
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Identification of a high-affinity-binding oligosaccharide by (+) nanoelectrospray quadrupole time-of-flight tandem mass spectrometry of a noncovalent enzyme-ligand complex
Y1  - 2006
UR  - http://www3.interscience.wiley.com/cgi-bin/jhome/26737/
U6  - https://doi.org/10.1002/anie.200503168
SN  - 1433-7851
ER  - 
TY  - JOUR
A1  - Haebel, Sophie
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Mass spectrometry of chitooligosaccharides
Y1  - 1997
SN  - 88-86889- 01-1
ER  - 
TY  - JOUR
A1  - Letzel, Matthias C.
A1  - Synstad, Bjoenar
A1  - Eijsink, Vincent G. H.
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Libraries of chito-oligosaccharides of mixed acetylation patterns and their interactions with chitinases
Y1  - 1999
SN  - 3-9806494-5-8
ER  - 
TY  - JOUR
A1  - Letzel, Matthias C.
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Mass spectrometry of chitin and chitosan oligosaccharides
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Bahrke, Sven
A1  - Einarsson, Jon M.
A1  - Gislason, Johannes
A1  - Haebel, Sophie
A1  - Letzel, Matthias C.
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Sequence analysis of chitooligosaccharides by matrix-assisted laser desorption ionization postsource decay mass spectrometry
N2  - Oligosaccharides composed of 2-acetamido-2-deoxy-D-glucopyranose (GlcNAc) and/or 2-amino-2-deoxy-D- glucopyranose (GlcN) were prepd. by chem. degrdn. of chitin or chitosan and sepd. by gel permeation chromatog. Oligosaccharides obtained after enzymic hydrolysis of chitosan [FA 0.19] with a fungal chitinase were derivatized by reductive amination with 2-aminoacridone and sequenced by matrix-assisted laser desorption ionization time-of-flight postsource decay (PSD) mass spectrometry (MS). The sequence of a trimer, D1A2, was established as D-A-A. The compn. of a hexamer D3A3 was .apprx.65% D-A-D-D-A-A and 35% D-D-A-D-A-A. The PSD MS of a nonamer D5A4-amac revealed four isobaric species D-X-Y-D-X-Y-D-A-A, where A is GlcNAc, D is GlcN, and X and Y (X ¹ Y) are mutually either D or A. This structure motif was also obsd. in a dodecamer D7A5 which was composed of eight isobaric sequences of the general formula (D-X-Y)3- D-A-A.
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Bahrke, Sven
A1  - Einarsson, Jon M.
A1  - Gislason, Johannes
A1  - Haebel, Sophie
A1  - Peter-Katalinic, Jasna
T1  - Characterization of chitooligosaccharides by mass spectrometry
N2  - Heterochitooligosaccharides of DP 6, DP 9, and DP 12 were evaluated using established methods of derivatization and matrix-assisted laser desorption ionization post source decay mass spectrometry.
Y1  - 2003
SN  - 82-471-5901-5
ER  - 
TY  - JOUR
A1  - Stalz, Holger
A1  - Roth, Udo
A1  - Schleuder, Detlev
A1  - Macht, Marcus
A1  - Haebel, Sophie
A1  - Strupat, Kerstin
A1  - Peter-Katalinic, Jasna
A1  - Hanisch, Franz-Georg
T1  - The Geodia cydonium galectin exhibits prototype and chimera-type characteristics and a unique sequence polymorphism within its carbohydrate recognition domain
N2  - The ancestral galectin from the sponge Geodia cydonium (GCG) is classified on a structural basis to the prototype subfamily, whereas its carbohydrate-binding specificity is related to that of the mammalian chimera-type galectin-3. This dual coordination reveals GCG as a potential precursor of the later evolved galectin subfamilies, which is reflected in the primary structure of the protein. This study provides evidence that GCG is the LECT1 gene product, while neither a previously described LECT2 gene nor a functional LECT2 gene product was found in the specimen under investigation. The electrophoretically separated protein isomers with apparent molecular masses of 13, 15, and 16 kDa correspond to variants of the LECT1 protein-exhibiting peptide sequence polymorphisms that concern critical positions of the carbohydrate recognition domain (13 kDa: Leu51, Asn55, His130, Gly137; 15 kDa: Ser51, Asn55, Asn130, Gly137; 16 kDa: Ser51, Tyr55, Asn130, Glu137). Four residues, highly conserved in the galectin family, are substituted. None of the residues claimed to be involved in interactions with GalNAc alpha 1-3 moieties at an extended binding subsite of galectin-3 was identified in the corresponding positions of GCG. Apparently, the substitutions do not confer distinct binding characteristics to the GCG variants as evidenced by binding studies with a recombinantly expressed 15-kDa isoform. The natural isoforms as well as the recombinant 15-kDa isoform oligomerize by the formation of non-covalent heteromeric or homomeric complexes. A phosphorylation of the galectin was confirmed neither by mass spectrometry nor by alkaline phosphatase treatment combined with isoelectric focusing
Y1  - 2006
UR  - http://glycob.oxfordjournals.org/content/16/5/402.full
U6  - https://doi.org/10.1093/glycob/cwj086
ER  -