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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 for "feed-forward activation" (FFA). The point is made of the approach used to demonstrate why peptide amino acids "boost" yields in microbial cell protein (MCP) synthesis. Whether boosted cellular proteasomes can be a significant player and at what stage of cell growth and development, is still open to question at this time.
In excess or damaged proteins supplied in rumen microbial cells can be acted on by proteasomal lysis, the resulting 'catalytic' effect by peptides is to have one at the downward cycling of the diurnal feeding phasic curves with cell protein synthesized and not as their asymptotic 'saturation'.
Enzyme protein polymerase's feed forward activation (FFA) is the only possibility to explain the boosting effect of pre-formed amino acids (PFAAs), peptides compared to their amino acids, on protein synthesis in the rumen. This sets it as the precedent to this later posit of FFA. 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, e. g. facilitated diffusion, and during diurnal cycling with feeding, evolved to hasten the process of MCP synthesis in a highly competitive environment, which would otherwise 'wash 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 graded 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 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. The nature of allosteric activation (opposite to inhibition) is a 1:1 relationship between [E] and [A], i. e. the enzyme-activator complex is mole by mole converted to activated status and is believed to be multiplicative in principal as expressed in this rate eqn. regards the FFA model. Here is the model on which Eqn. [1] is based upon as given, previously: [E] + [S] + [S] <=> [E][S][S] -> [P] ^ ^ || +[A] || +[A] v +[S] v [E][A] <=> [E][S][S][A] +[S] Concluding Remarks. 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). Importantly, there is a stipulation that allosteric inhibition is probably highly coordinated within tertiary subunit structure in the protein polymerase. This subsumes a more intricate interactive modeled mechanism where multiple units are factored in when the allosteric activator binds and activates the active site of the polymerase enzyme. Furthermore, studies are needed to elucidate the protein polymerases in given hosts such as ruminal proteolytics and fibrolytics for microbes in FFA (feed-forward activation) which can be manipulated as such as those microbial populations subsisting in hypercompetitive environments for either: 1) substrates and/or 2) extreme temps. (hot/cold) and pH (acid) specific e. g. being in: 1) the cow's rumen stomach, 2) hindgut of the equine, 3) cold immersive environments (ICE) as in Ocean depths near the Artic, 4) hot springs or Ocean vents in the sea floor and 5) municipal sewage sludge (MSS) and still speculatively peptide additives for man made fermentation as in 1) ensilage involving preservation to stability of the fodder biomass and 2) composting of green biomass in order to breakdown to stability after the initial process. (c) 2026-2059. Skye Blue Press Corporation. Poco, Colombie-Britannique, V3B 1G3 Canada.
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Last update of this entry: April 18, 2026
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