John F. Morrison

Affiliations: 
Australian National University, Acton, Australian Capital Territory, Australia 
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"John F. Morrison"
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MORRISON JF. (2003) The kinetics of the reactions catalyzed by aconitase. The Australian Journal of Experimental Biology and Medical Science. 32: 867-76
MORRISON JF, O'SULLIVAN WJ. (1996) KINETIC STUDIES OF THE REVERSE REACTION CATALYSED BY ADENOSINE TRIPHOSPHATE-CREATINE PHOSPHOTRANSFERASE. THE INHIBITION BY MAGNESIUM IONS AND ADENOSINE DIPHOSPHATE. The Biochemical Journal. 94: 221-35
Sculley MJ, Morrison JF, Cleland WW. (1996) Slow-binding inhibition: the general case. Biochimica Et Biophysica Acta. 1298: 78-86
Williams EA, Morrison JF. (1992) Human dihydrofolate reductase: reduction of alternative substrates, pH effects, and inhibition by deazafolates. Biochemistry. 31: 6801-11
Williams EA, Morrison JF. (1991) Characterization of tightly bound substrates in pure preparations of dihydrofolate reductase: implications for studies on enzymes. Biochimica Et Biophysica Acta. 1078: 47-55
Turnbull J, Morrison JF, Cleland WW. (1991) Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by L-tyrosine. Biochemistry. 30: 7783-8
Turnbull J, Cleland WW, Morrison JF. (1991) pH dependency of the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli. Biochemistry. 30: 7777-82
Turnbull J, Morrison JF. (1990) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 2. Evidence for two different active sites. Biochemistry. 29: 10255-61
Turnbull J, Cleland WW, Morrison JF. (1990) Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 1. Kinetic characterization of the dehydrogenase reaction by use of alternative substrates. Biochemistry. 29: 10245-54
Morrison JF, Walsh CT. (1988) The behavior and significance of slow-binding enzyme inhibitors. Advances in Enzymology and Related Areas of Molecular Biology. 61: 201-301
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