Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Ditmar G. E. Lubini"'
Autor:
Philipp Christen, Ditmar G. E. Lubini
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 76(6)
Paracatalytic enzyme modifications result from the oxidation of enzyme—substrate carbanions by extrinsic oxidants. During the oxidation of enzyme-activated substrates, transiently reactive intermediates are generated which, without being released f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8708e61fac3c1c7ec29338741aeb8ef
https://pubmed.ncbi.nlm.nih.gov/288042
https://pubmed.ncbi.nlm.nih.gov/288042
Publikováno v:
European journal of biochemistry. 63(1)
Four different enzymes, class I fructose-1,6-bisphosphate aldolase from rabbit muscle, class II fructose-l,6-bisphosphate aldolase from yeast, transaldolase, and transketolase, are inactivated progressively in the presence of their specific substrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f91dd433e3e6eb36ad29f66ee4d41f01
https://pubmed.ncbi.nlm.nih.gov/770167
https://pubmed.ncbi.nlm.nih.gov/770167
Publikováno v:
Experientia. 33(6)
Fructose-1,6-P2 was immobilized by sodium borohydride reduction of the Schiff base formed with aminated agarose (AH-Sepharose 4B®). The coupling occurs with high yield (25 μmoles immobilized fructose-1,6-P2 per ml packed gel) at neutral pH and room
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7abdacbfe824aad22cae022c239df51f
https://pubmed.ncbi.nlm.nih.gov/330192
https://pubmed.ncbi.nlm.nih.gov/330192