E
Eric G. Brown
Researcher at Swansea University
Publications - 42
Citations - 815
Eric G. Brown is an academic researcher from Swansea University. The author has contributed to research in topics: Cyclic nucleotide phosphodiesterase & Phosphodiesterase. The author has an hindex of 16, co-authored 42 publications receiving 804 citations. Previous affiliations of Eric G. Brown include University of Siena.
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Biosynthesis of anatoxin-a by Anabaena flos-aquae: Examination of primary enzymic steps
TL;DR: The arginine and ornithine decarboxylases required to produce putrescine, and a diamine oxidase to cyclize it to Δ 1 -pyrroline, were shown to be active in A. flos-aquae IC-1 and it is suggested that this, together with their chromatographic coincidence, may indicate a single protein.
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Adenosine 3′:5′-cyclic monophosphate, adenylate cyclase and a cyclic AMP binding-protein in Phaseolus vulgaris
TL;DR: The validity of using the binding-protein method for determining cyclic AMP in purified and partially purified extracts of Phaseolus tissues has been examined and confirmed and isolated intact chloroplasts were shown to possess adenylate cyclase activity.
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The cyclic nucleotide phosphodiesterases of spinach chloroplasts and microsomes
TL;DR: Electrophoresis after dissociation indicates that 1 c and 1 m are both enzyme complexes being involved in the metabolism of 3′:5′-cyclic AMP, and the 1 m complex being concerned with RNA catabolism.
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Identification of cyclic nucleotide constituents of meristematic and non-meristematic tissue of Pisum sativum roots
Russell P. Newton,Donato Chiatante,Dipankar Ghosh,A. Gareth Brenton,Terence J. Walton,Frank M. Harris,Eric G. Brown +6 more
TL;DR: 3′,5′-Cyclic-AMP, -GMP, -CMP and -UMP were found to be present in Pisum meristematic tissue and 3′, 5′-cyclic-amp, -gMP,-CMP, –IMP and -DTMP are present in the non-meristematics regions.
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Plurality of cyclic nucleotide phosphodiesterase in Spinacea oleracea: subcellular distribution, partial purification, and properties
TL;DR: Evidence is presented that an endogenous activator is also present in the spinach homogenate and that the phosphodiesterase of highest specific activity is located in the peroxisomes but that an enzyme of relatively high specific activity also occurs in the chloroplast and Golgi fractions.