Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Graham F. Betts"'
Autor:
Graham F. Betts, Lois M. Levy
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 832:186-191
It has been shown by deLooze and Wagner (Physiol. Plant. 57 (1983) 243–249) that the association/dissociation phenomena of NADP-dependent d -glyceraldehyde-3-phosphate oxidoreductase (phosphorylating) ( d -glyceraldehyde-3-phosphate:NADP+ oxidoredu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ab4b06bd71b359e7affb2d7d4b40dfd
https://doi.org/10.1016/0167-4838(85)90330-9
https://doi.org/10.1016/0167-4838(85)90330-9
Autor:
Graham F. Betts, Harold J. Evans
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 167:190-193
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::709761dbd1020f3d9a4a271497500d33
https://doi.org/10.1016/0005-2744(68)90291-x
https://doi.org/10.1016/0005-2744(68)90291-x
Autor:
Graham F. Betts, Harold J. Evans
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 167:193-196
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15ac8dba37a9f80ddac8817a82308149
https://doi.org/10.1016/0005-2744(68)90292-1
https://doi.org/10.1016/0005-2744(68)90292-1
Autor:
Graham F. Betts, Lois M. Levy
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 997:331-333
The stereospecificity of the reaction catalysed by the spinach chloroplast enzyme NADP-dependent glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate: NADP+ oxidoreductase (phosphorylating), EC 1.2.1.13) with respect to the C4 nicot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5d5d15ba28582f2d531dfa82976fc78
https://doi.org/10.1016/0167-4838(89)90204-5
https://doi.org/10.1016/0167-4838(89)90204-5
Autor:
Graham F. Betts, Ralf Landgraf
Publikováno v:
Analytical biochemistry. 176(2)
A rapid double mixing technique has been applied to the reaction kinetics of enzymes usually analyzed by linked assay. The test enzyme is allowed to perform in the absence of the linking enzyme but then the convenience of enzymatic analysis of accumu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a474bd66b3d24915a7386648ba434d0
https://pubmed.ncbi.nlm.nih.gov/2742135
https://pubmed.ncbi.nlm.nih.gov/2742135
Autor:
Lois M. Levy, Graham F. Betts
Publikováno v:
Biochimica et biophysica acta. 955(2)
The ability of NADPH to compete for binding with other ligands of known affinity has been used to provide values for the Kd of NADPH with ferredoxin-NADP+ oxidoreductase (EC 1.18.1.2) (FNR). When the competing ligand is procion red, which binds with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e7900aff71157381b44a1f4ccef10be
https://pubmed.ncbi.nlm.nih.gov/3395627
https://pubmed.ncbi.nlm.nih.gov/3395627
Autor:
Mary G. Springham, Graham F. Betts
Publikováno v:
Biochimica et biophysica acta. 309(1)
The activity of aldehyde dehydrogenase decreases following dilution of activating K+, or addition of Li+ which is competitive with K+, at a rate which is considerably smaller than the likely rate of K+ dissociation from the enzyme. These results are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ac627efa95a3a3d65ad0b4ccc9ac0ec
https://pubmed.ncbi.nlm.nih.gov/4575348
https://pubmed.ncbi.nlm.nih.gov/4575348