Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Esther Schweinzer"'
Publikováno v:
Cell Biochemistry and Function. 14:27-31
K562 erythroleukaemic cells produced ascorbate when incubated with dehydroascorbic acid. The reduction depended on the number of cells and on the concentration of dehydroascorbic acid. The observed rate consists of a high affinity (apparent Km 7 mu M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d238336878940cf0ff65793710fc361
https://doi.org/10.1002/cbf.635
https://doi.org/10.1002/cbf.635
Autor:
Hans Goldenberg, Esther Schweinzer
Publikováno v:
Journal of Bioenergetics and Biomembranes. 26:359-367
The transport systems of animal and human tissues for vitamin C are reviewed with respect to their properties. It emerges that pure diffusion plays only a very minor role, while a variety of more or less specific transporters is found on cellular mem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9c9c9d941409baf7d3cd9f41f0cc73c
https://doi.org/10.1007/bf00762776
https://doi.org/10.1007/bf00762776
Autor:
Esther Schweinzer, Hans Goldenberg
Publikováno v:
European Journal of Biochemistry. 218:1057-1062
A transmembrane monodehydroascorbate reductase activity with a high affinity in the subpicomolar concentration range of the free radical can be measured at the surface of erythroleukemic cells using a ferricyanide-driven redox cycle. The activity is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c897edf429fcd0e3f72e1addca217ca
https://doi.org/10.1111/j.1432-1033.1993.tb18465.x
https://doi.org/10.1111/j.1432-1033.1993.tb18465.x
Autor:
Alajos Bérczi, Monika Fritzer, Viktória Szűts, Esther Schweinzer, Hans Goldenberg, Monika Ruthner
Publikováno v:
European journal of biochemistry. 213(1)
The influence of conjugation of doxorubicin to holotransferrin on the receptor-mediated endocytosis of and on the iron uptake from transferrin was studied using K562 cells. 125I-labelled transferrin and doxorubicin-transferrin conjugates were used in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::834257ed86cbebfbc706686becb50eb7
https://pubmed.ncbi.nlm.nih.gov/8477715
https://pubmed.ncbi.nlm.nih.gov/8477715
Autor:
Esther Schweinzer, Hans Goldenberg
Publikováno v:
European journal of biochemistry. 206(3)
Transmembrane reduction of extracellular oxidants by K562 and U937 leukemic cells was stimulated by catalytic amounts of ascorbate or dehydroascorbate. This stimulation was not due to transport of ascorbate in different redox states in and out of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14f247c2edad1c51d43cc3e5dd0cce98
https://pubmed.ncbi.nlm.nih.gov/1606963
https://pubmed.ncbi.nlm.nih.gov/1606963
Publikováno v:
FEBS Letters. (1):106-108
We disprove that living cells stabilize ascorbate by the activity of a trans plasma membrane semidehydroascorbate reductase. The two processes show different specificities for both substrate and inhibitor. Not only cells but also cell-conditioned buf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::645c99b9b519a92233bb1d1e285473c6
Autor:
Thomas. Moslinger, Leopold Jirovetz, Paul Krajnik, Hans Goldenberg, Esther Schweinzer, Wilhelm. Mosgoeller
Publikováno v:
ResearcherID
Micromolar concentrations of dehydroascorbic acid in aqueous solutions react with methanol-containing phosphate or citrate buffers to form a mixture of derivatives with an absorption maximum at 346 nm. The compounds, different methyl ketals, were ana
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3787ed1afb14cb431b0d8b414f3fc0f8
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1994ND41500027&KeyUID=WOS:A1994ND41500027
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=ORCID&SrcApp=OrcidOrg&DestLinkType=FullRecord&DestApp=WOS_CPL&KeyUT=WOS:A1994ND41500027&KeyUID=WOS:A1994ND41500027
