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Enzyme Hydrolyzed Collagen Protein
Enzyme Hydrolyzed Collagen Protein

... the human body and in the same sizes and amounts the human body utilizes (making it the most bioidentical). The low-temperature, gentle drying cycle ensures that biologically active state of all cofactors and amino acids peptides remain intact. Thus the end product will have a higher concentration o ...
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this PDF file - Periodica Polytechnica
this PDF file - Periodica Polytechnica

... of both cereals treated with N showed the highest contents. Important PK dosages were seen to markedly reduce the content of most amino acids, in particular, glutamic acid (GLU). The lowest amino acid contents were found in triticale for PK treatment, while in rye for NP2K2 treatment. All the essent ...
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Name: Date: Transcription and Translation Worksheet – ANSWER

... was changed to thymine, would the final protein change? Why? No. Initially, the DNA strand had the triplet TTC – this created the mRNA codon AAG. If we change the template to TTT, the new codon would be AAA. Both AAG and AAA code for lysine, so the final protein should still turn out the same (thank ...
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... As enzymes are made of protein, they have a particular 3D shape, and all enzymes have specific active sites that allow them to act on only one type of substance. Enzymes have an affinity to their substrate molecule. As the two combine, the shape of the active site changes slightly – this is known a ...
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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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