Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1971 Mar;122(1):18P–19P. doi: 10.1042/bj1220018pb

Kinetics and inhibition by adenosine phosphates and nitrite of nitrate reductase from Spinacea oleracea L.

A R Eaglesham, E J Hewitt
PMCID: PMC1176721  PMID: 4330963

Full text

PDF
18P

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim Biophys Acta. 1963 Jan 8;67:104–137. doi: 10.1016/0006-3002(63)91800-6. [DOI] [PubMed] [Google Scholar]
  2. CLELAND W. W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory. Biochim Biophys Acta. 1963 Feb 12;67:173–187. doi: 10.1016/0006-3002(63)91815-8. [DOI] [PubMed] [Google Scholar]
  3. CRESSWELL C. F., HAGEMAN R. H., HEWITT E. J., HUCKLESBY D. P. THE REDUCTION OF NITRATE, NITRITE AND HYDROXYLAMINE TO AMMONIA BY ENZYMES FROM CUCURBITA PEPO L. IN THE PRESENCE OF REDUCED BENZYL VIOLOGEN AS ELECTRON DONOR. Biochem J. 1965 Jan;94:40–53. doi: 10.1042/bj0940040. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. FLORINI J. R., VESTLING C. S. Graphical determination of the dissociation constants for two-substrate enzyme systems. Biochim Biophys Acta. 1957 Sep;25(3):575–578. doi: 10.1016/0006-3002(57)90529-2. [DOI] [PubMed] [Google Scholar]
  5. Levitzki A., Koshland D. E., Jr Negative cooperativity in regulatory enzymes. Proc Natl Acad Sci U S A. 1969 Apr;62(4):1121–1128. doi: 10.1073/pnas.62.4.1121. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES