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Chapter 1 – name - Nutrition Gardener
Chapter 1 – name - Nutrition Gardener

... What is the usual fate of orally ingested enzyme supplements? a. Digested by gastrointestinal proteases b. Rapidly degraded by salivary secretions c. Mostly absorbed in original form from stomach d. Completely absorbed in original form from jejunum ...
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... • tRNA molecules bring amino acids to the mRNA. • Peptide bonds form between an amino acid and the end of the growing peptide chain. • The ribosome moves along mRNA until the end of the codon (translocation). • The polypeptide chain is released from the ribosome and becomes an active protein. Someti ...
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... catabolism to provide amino acids, not only as substrates for gluconeogenesis, but also as the main metabolic fuel of all tissues. Death results when essential tissue proteins are catabolized and not replaced. In patients with cachexia as a result of release of cytokines in response to tumors and a ...
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Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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