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CONTACT - Our Own E-Newsletter on Curent Events, Science and Nature Vol. I, Issue No. 1 April 04, 2026 Fast-Forward Activation (FFA): a first in microbial mechanistic polymerase action for the competitive rumen environment. By D. A. Flores SB Internet, Poco, BC Canada V3B 1G3 To continue to a more comprehensive Protein Energy Theory for ruminal digestion and nutrition, ff. this is to be our mechanical kinetic calculations for the chaperoning with peptides to cellular microbial protein synthesis describing a new phenomenon of "feed-forward activation" (FFA). The point is made of the approach used to demonstrate why peptide amino acids being about "boosted" yields in microbial cell protein (MCP) synthesis. Whether boosted proteasomes can be a significant player and at what stage of cell growth and development, is still open to question at this time. The hypothesis states that boosting is dependent to feeding and reaches "saturation" maximally without further yield at their azimuth or peak but the pattenr of in phase, nested curves that is expected is open to question and could be either simply parallel or used at their azimuth and the shoulders eventually. It is believed by scientists that a comprehensive rumen Protein Energy Theory can be proven utilizing feed-grade rumen affinity resins for peptides/A.A.'s availability and transport and regulating proteasomal equilibrium through native peptide turnover & FFA with microbial cells. Read on also along our story regards nutri-pharma and human and animal nutrition including our interest in class nutraceuticals: oligosaccharides and oligopeptides and activated VitD 2,3-agonist in the upper and lower gut of animals, for the former 2, an the lower gut and post-absorptively for the latter, what will become major nutraceuticals, as we predict. It is believed by concensus by scientists that a comprehensive Protein Energy Theory of the rumen stomach, a "dynamo" of protein synthesis, can be approached and studied with use of: 1) feed-grade rumen affinity resins for peptide/A.A. availability for transport, and 2) resetting proteasomal equilibrium for native peptide turnover from excess or damaged intracellular microbial protein and their kinetic process of feed-forward activation (FFA) there in microbial cells. Proteomics with peptide studies of their distribution from source dietary proteins in vitro including sequencing will determine the primary structure of critical amino acids and their sequences allowing allosteric interaction with model rumen microbial polymerases that constitute a feed-forward activation (FFA) mechanism for rumen microbial metabolism. Taking a look at the situation, peptides are ushered into the cell by transport processes, and during diurnal cycling with feeding, evolved to hasten the process of MCP synthesis in a highly competitive environment, otherwise 'washing out' from the rumen stomach to no avail. In vitro studies modeling polymerases from rumen microbes and their protein end products will be measured at the appropriate time-span with sampling after being 'stopped frozen' in time to measure their gradded effects with our chosen 'catalytic' peptides. A designed microbial cell system (proteolytic + fibrolytic) with complete source medium from rumen sampling will be used for the in vitro model system in this experiment with graded dosage by our chosen 'catalytic' peptide spp.. alone or in concert. To continue featuring here the new and unique occurence of fast forward activation (FFA) in microbial metabolism we believe is just the beginning for highly selective ecological environments like the rumen and other environments that pose harsher conditions than normal such as hot undersea vents on the Ocean's floor and whose kinetics for their protein polymerases and 'catalytic' peptides are allosteric, opposite to that of non-competitive (allosteric-type) inhibition using the basic equation: v (rate or velocity of rxn) = k [S]2 * [Polymer]0 * [A], Eqn. [1], where k=rate constant of this second order rxn, [A]=activator or peptide 'catalytic' player or agent, [S]=monomeric amino acid concentration of which there are 21 independent-acting pools for each amino acid type which can vary with post-prandial, diurnal intake in the rumen milieu and [Polymer] is the primer/polymer concentration by extension and represents a constant value. Here is the model on which Eqn. [1] is based upon as given, previously: [E] + [S] <=> [E][S] -> [P] ^ ^ || +[A] || +[A] v +[S] v [E][A] <=> [E][S][A] E. g. s. of other classes of microbes are: 1) lithotrophs (ion spp. for energy), 2) autotrophs (inorganic cpds. for energy), phototrophs (hv or light as energy) and our own heterotrophs (using carbon-based substrates for energy). And finally importantly, there is a stipulation that allosteric inhibtion is probably highly coordinated within tertiary subunit structure in the protein polymerase. Further studies are needed to elucidate protein polymerases in given hosts such as ruminal proteolytics and fibrolytics, hot vents on the Ocean's floor and mesophilic digesters (from municipal sludge waste). (c) 2026-2059. Skye Blue Press Corporation. Poco, Colombie-Britannique, V3B 1G3 Canada.
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Last update of this entry: April 04, 2026
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