Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Susanne Jacobitz"'
Autor:
Gilbert Scott, Robert W. Colman, George A. Omburo, Theodore J. Torphy, Susanne Jacobitz, Roberta F. Colman
Publikováno v:
Blood. 89:1019-1026
Two cAMP analogs, 8- and 2- [(4-bromo-2,3-dioxobutyl) thio]adenosine 3′,5′-cyclic monophosphate (8- and 2-BDB-TcAMP) have been used in probing the catalytic site of recombinant monocyte cAMP-specific phosphodiesterase (PDE4a). 2-BDB-TcAMP is a re
Publikováno v:
FEMS Microbiology Letters. 87:253-260
The list of carboxydotrophic bacteria is constantly growing and we have found that burning charcoal piles harbor an especially rich CO-oxidizing microflora. The newly isolated Streptomyces thermoautotrophicus UBT1 is particularly interesting as it is
Autor:
Walter E. DeWolf, Theodore J. Torphy, Susanne Jacobitz, Ryan M Dominic, Megan M. McLaughlin, George P. Livi
Publikováno v:
Molecular pharmacology. 51(6)
To identify critical amino acids within the central conserved region of recombinant human cAMP-specific phosphodiesterase 4 subtype A (rhPDE4A), we engineered the expression of point mutants in a fully active rhPDE4A/Met201-886. When histidine residu
Autor:
Susanne Jacobitz, Ortwin Meyer
Publikováno v:
Archives of Microbiology. 145:372-377
In cell suspensions of Pseudomonas carboxydovorans pulsed with lithotrophic substrates (CO or H2) in the presence of oxygen, formation of reduced pyridine nucleotides and of ATP could be demonstrated using the bioluminescent assay. Experiments employ
Publikováno v:
FEMS Microbiology Letters. 28:141-144
Cells of Pseudomonas carboxydovorans from the exponential growth phase revealed the major portion (87%) of CO dehydrogenase attached to the inner aspect of the cytoplasmic membrane. In stationary cells only about half of the total amount of the enzym
Publikováno v:
FEMS Microbiology Letters. 39:161-179
The use of CO as a growth substrate by aerobic CO-oxidizing (carboxydotrophic) bacteria requires some features not obvious in other bacteria. These are the presence of the enzyme CO dehydrogenase, a branched respiratory chain with an alternative CO-i