Matches in UGent Biblio for { <https://biblio.ugent.be/publication/173540#aggregation> ?p ?o. }
Showing items 1 to 37 of
37
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B41276.
- aggregation creator B41277.
- aggregation creator B41278.
- aggregation creator B41279.
- aggregation creator B41280.
- aggregation creator person.
- aggregation date "1999".
- aggregation format "application/pdf".
- aggregation hasFormat 173540.bibtex.
- aggregation hasFormat 173540.csv.
- aggregation hasFormat 173540.dc.
- aggregation hasFormat 173540.didl.
- aggregation hasFormat 173540.doc.
- aggregation hasFormat 173540.json.
- aggregation hasFormat 173540.mets.
- aggregation hasFormat 173540.mods.
- aggregation hasFormat 173540.rdf.
- aggregation hasFormat 173540.ris.
- aggregation hasFormat 173540.txt.
- aggregation hasFormat 173540.xls.
- aggregation hasFormat 173540.yaml.
- aggregation isPartOf urn:issn:0032-0935.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Maize glutathione-dependent formaldehyde dehydrogenase: protein sequence and catalytic properties".
- aggregation abstract "Glutathione-dependent formaldehyde dehydrogenase (FDH; EC 1.2.1.1) has been purified 3900-fold from maize cell-suspension cultures to a specific activity of 4.68 mu mol (mg protein)(-1) min(-1). The homogeneous enzyme consisted of two identical subunits with a molecular mass of 42 kDa, and an isoelectric point of 5.8. Eight tryptic peptides were sequenced and gave a perfect fit to the protein sequence derived from maize Fdh cDNA (J. Fliegmann and H. Sandermann, 1997, Slant Mol Biol 34: 843-854). There was 62% identity with the eucaryotic FDH consensus sequence. Michaelis constants of approx. 20 mu m (formaldehyde), approx; 50 mu m (glutathione) and approx. 31 mu m (NAD(+)) were determined for the maize enzyme as well as for FDH partially purified from dog lung. Besides S-hydroxymethylglutathione, pentanol-1, octanol-1, and omega-hydroxy-fatty acids served as substrates for both FDH preparations. The unusual substrate specificity indicates that FDH may be involved in the detoxification of long-chain lipid peroxidation products.".
- aggregation authorList BK104390.
- aggregation endPage "18".
- aggregation issue "1".
- aggregation startPage "12".
- aggregation volume "208".
- aggregation aggregates 4151843.
- aggregation isDescribedBy 173540.
- aggregation similarTo s004250050529.
- aggregation similarTo LU-173540.