Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Lieselotte Leuschel"'
Publikováno v:
FEBS Letters. 227:1-4
In proteins released from quiescent human neutrophils during incubation, 21% of the methionine (Met) residues were found to be oxidized. However, the portion of oxidized Met in extracellular proteins increased to 66% after stimulating the cells with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3f909239b2420968382e3b143d8d913
https://doi.org/10.1016/0014-5793(88)81401-7
https://doi.org/10.1016/0014-5793(88)81401-7
Autor:
Ingrid Beck-Speier, Hans Weber, Lieselotte Leuschel, Konrad Maier, Eva Matejkova, Helga Hinze
Publikováno v:
FEBS Lett. 250, 221-226 (1989)
Oxidation of the reactive site methionine (Met) in α-1-proteinase inhibitor (α-1-PI) to methionine sulfoxide (Met(O)) is known to cause depletion of its elastase inhibitory activity. To estimate the selectivity of different oxidants in converting M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82a201dc1a06226d3f284341ea6b2e00
https://doi.org/10.1016/0014-5793(89)80725-2
https://doi.org/10.1016/0014-5793(89)80725-2
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 848:120-130
The pools of ribonucleoside di- and triphosphates decrease within a few min after addition of 5 mM sulfite to a suspension of Saccharomyces cerevisiae at pH 3.6. Levels of the corresponding ribonucleoside monophosphates increase in parallel. The stro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ffec54ef2cb2ed8f3fb628e2dc29abf1
https://doi.org/10.1016/0005-2728(86)90167-2
https://doi.org/10.1016/0005-2728(86)90167-2
Publikováno v:
Journal of chromatography. 493(2)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fdf9f8e2b6915fc42ea78b3465b18d7
https://pubmed.ncbi.nlm.nih.gov/2584304
https://pubmed.ncbi.nlm.nih.gov/2584304
Publikováno v:
Biochimica et biophysica acta. 661(1)
The substrate specificity of proteinase B (EC 3.4.22.9) from Baker's yeast was studied. Experiments with unblocked synthetic peptides indicated that the enzyme has no aminopeptidase activity. The proteinase cleaves trypsin substrates like Bz-Arg-OEt,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30737b3275829a65d015f218cd9b2065
https://pubmed.ncbi.nlm.nih.gov/7028121
https://pubmed.ncbi.nlm.nih.gov/7028121