F
F. John Ballard
Researcher at Commonwealth Scientific and Industrial Research Organisation
Publications - 18
Citations - 1337
F. John Ballard is an academic researcher from Commonwealth Scientific and Industrial Research Organisation. The author has contributed to research in topics: Insulin-like growth factor & Protein degradation. The author has an hindex of 12, co-authored 18 publications receiving 1305 citations. Previous affiliations of F. John Ballard include Flinders University.
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Production and utilization of acetate in mammals
TL;DR: It is proposed that acetate in the blood of rats or starved sheep is derived from the hydrolysis of acetyl-CoA, and release of acetate from tissues would occur under conditions when the function of the tricarboxylic acid cycle is restricted.
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Inhibition of protein degradation in isolated rat hepatocytes
TL;DR: The sensitivity of proteolysis in isolated hepatocytes to these various inhibitory agents is discussed in relation to their possible modes of action.
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New Opportunities from the Isolation and Utilization of Whey Proteins
Geoffrey W. Smithers,F. John Ballard,Adam D. Copeland,Kirthi De Silva,David A. Dionysius,G L Francis,Chris Goddard,Paul A. Grieve,Graeme H. McIntosh,Ian R. Mitchell,R. John Pearce,Geoffrey Owen Regester +11 more
TL;DR: Although whey represents a rich source of proteins with diverse food properties for nutritional, biological, and functional applications, commercial exploitation of these proteins has not been widespread because of a restricted applications base, a lack of viable industrial technologies for protein fractionation, and inconsistency in product quality.
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The bovine insulin-like growth factor (IGF) binding protein purified from conditioned medium requires the N-terminal tripeptide in IGF-1 for binding
TL;DR: The N-terminal destripeptide truncated form of bovine IGF-1, which has enhanced biological activity, was found to have a markedly reduced affinity for BP compared to intact IGF- 1.
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Natural and synthetic forms of insulin-like growth factor-1 (IGF-1) and the potent derivative, destripeptide IGF-1: biological activities and receptor binding.
TL;DR: IGF-1, whether recombinant, chemically-synthesised or purified from bovine colostrum, was equipotent in radioreceptor assays with IGF-1 or insulin-like growth factor-2 as radioligand as well as in its ability to stimulate protein synthesis in L6 myoblasts.