Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Silke Schrader"'
Publikováno v:
Journal of Biological Chemistry. 278:23301-23310
Trypanosomes express an enzyme called trans-sialidase (TS), which enables the parasites to transfer sialic acids from the environment onto trypanosomal surface molecules. Here we describe the purification and characterization of two TS forms from the
Autor:
Silke Schrader, Jörg J. Sauter
Publikováno v:
Journal of Plant Physiology. 159:833-843
Summary Two important enzymes of sucrose metabolism, sucrose-phosphate synthase (SPS, EC 2.4.1.14) and sucrose synthase (SuSy, EC 2.4.1.13), were investigated in the ray parenchyma cells of the trunk wood of Populus × canadensis Moench ‘robusta’
Publikováno v:
Physiologia Plantarum. 97:402-410
Nitrogen represents a critical nutrient in raised bogs. In Sphagna, dominating this habitat, the prevalent storage amino acid asparagine is catabolized predominantly by the enzyme L-asparaginase (EC 3.5.1.1). L-asparaginase activity has been detected
Autor:
Silke Schrader, Udo Johanningmeier
Publikováno v:
Plant Molecular Biology. 19:251-256
The D1-precursor protein of the photosystem II reaction centre contains a carboxy-terminal extension whose proteolytic removal is necessary for oxygen-evolving activity. To address the question of the role of the carboxy-terminal extension in the gre
Autor:
Silke, Schrader, Roland, Schauer
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 347
Trans-sialidase (TS; E.C. 3.2.1.18) catalyzes the transfer of preferably alpha2,3-linked sialic acid to another glycan or glycoconjugate, forming a new alpha2,3-linkage to galactose or N-acetylgalactosamine. In the absence of an appropriate acceptor,
Autor:
Roland Schauer, Silke Schrader
Trans-sialidase (TS; E.C. 3.2.1.18) catalyzes the transfer of preferably alpha2,3-linked sialic acid to another glycan or glycoconjugate, forming a new alpha2,3-linkage to galactose or N-acetylgalactosamine. In the absence of an appropriate acceptor,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5c1a58daedb521aeb01edb6aa910cac3
https://doi.org/10.1385/1-59745-167-3:93
https://doi.org/10.1385/1-59745-167-3:93
Publikováno v:
Analytical biochemistry. 322(2)
Trans-sialidase (E.C. 3.2.1.18) catalyzes the transfer of preferably alpha2,3-linked sialic acid to another glycan or glycoconjugate, forming a new alpha2,3 linkage to galactose or N-acetylgalactosamine. Here, we describe a nonradioactive 96-well pla
Autor:
Ulrich Mühlenhoff, Ursula Altenfeld, Heike Thomas, Matthias Rögner, Silke Schrader, Dirk Schneider
Publikováno v:
Biochimica et biophysica acta. 1491(1-3)
The genes encoding cytochrome f (petA), cytochrome b(6) (petB), the Rieske FeS-protein (petC), and subunit IV (petD) of the cytochrome b(6)f complex from the thermophilic cyanobacterium Synechococcus elongatus were cloned and sequenced. Similar to ot