Publications

A comparison of one-dimensional and two-dimensional NMR methods for measuring enzyme-catalyzed exchange

Authors: J Boyd, KM Brindle, ID Campbell, GK Radda

E-pub date: 15 Oct 1984

Journal name: Journal of Magnetic Resonance 1969

A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte.

Authors: ST Oxley, R Porteous, KM Brindle, J Boyd, ID Campbell

E-pub date: 14 Sep 1984

Journal name: Biochim Biophys Acta

1H NMR measurements of enzyme-catalyzed 15N-label exchange

Authors: KM Brindle, R Porteous, ID Campbell

E-pub date: 1 Aug 1984

Journal name: JOURNAL OF MAGNETIC RESONANCE

The inhibition of erythrocyte glyceraldehyde-3-phosphate dehydrogenase. In situ PMR studies.

Authors: DL Foxall, KM Brindle, ID Campbell, RJ Simpson

E-pub date: 19 Jun 1984

Journal name: Biochim Biophys Acta

A comparison of 31P-NMR saturation transfer and isotope-exchange measurements of creatine kinase kinetics in vitro.

Authors: KM Brindle, R Porteous, GK Radda

E-pub date: 27 Apr 1984

Journal name: Biochim Biophys Acta

Proton NMR measurements of hydrogen exchange at the C-3 position of 3-hydroxybutyrate in suspensions of rat liver mitochondria.

Authors: HH Paul, KM Brindle, ID Campbell, DJ Smith

E-pub date: 14 Nov 1983

Journal name: FEBS Lett

Isolation and characterisation of genomic and cDNA clones for an androgen-regulated secretory protein of rat seminal vesicles.

Authors: L Williams, C McDonald, S Jackson, E McIntosh, S Higgins

E-pub date: 11 Aug 1983

Journal name: Nucleic Acids Res

Centrifugal analysis of undiluted packed human erythrocyte lysates. Studies of the association of glyceraldehyde-phosphate dehydrogenase with the membrane fraction.

Authors: RJ Simpson, KM Brindle, ID Campbell

E-pub date: 29 Jul 1983

Journal name: Biochim Biophys Acta

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A comparison of one-dimensional and two-dimensional NMR methods for measuring enzyme-catalyzed exchange

A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte.

1H NMR measurements of enzyme-catalyzed 15N-label exchange

The inhibition of erythrocyte glyceraldehyde-3-phosphate dehydrogenase. In situ PMR studies.

A comparison of 31P-NMR saturation transfer and isotope-exchange measurements of creatine kinase kinetics in vitro.

Proton NMR measurements of hydrogen exchange at the C-3 position of 3-hydroxybutyrate in suspensions of rat liver mitochondria.

Isolation and characterisation of genomic and cDNA clones for an androgen-regulated secretory protein of rat seminal vesicles.

Centrifugal analysis of undiluted packed human erythrocyte lysates. Studies of the association of glyceraldehyde-phosphate dehydrogenase with the membrane fraction.

Themes

Filters

Research Groups

Core Facilities

Start date

End date

A comparison of one-dimensional and two-dimensional NMR methods for measuring enzyme-catalyzed exchange

A multinuclear NMR study of 2,3-bisphosphoglycerate metabolism in the human erythrocyte.

1H NMR measurements of enzyme-catalyzed 15N-label exchange

The inhibition of erythrocyte glyceraldehyde-3-phosphate dehydrogenase. In situ PMR studies.

A comparison of 31P-NMR saturation transfer and isotope-exchange measurements of creatine kinase kinetics in vitro.

Proton NMR measurements of hydrogen exchange at the C-3 position of 3-hydroxybutyrate in suspensions of rat liver mitochondria.

Isolation and characterisation of genomic and cDNA clones for an androgen-regulated secretory protein of rat seminal vesicles.

Centrifugal analysis of undiluted packed human erythrocyte lysates. Studies of the association of glyceraldehyde-phosphate dehydrogenase with the membrane fraction.