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- W362401545 abstract "More and more facts appear showing that there are oligopeptides in different organs and tissues of living organisms that are not formed from specialized precursors, but are rather natural fragments of well studied proteins. However, up to the present time practically no systemic structural and functional investigations of protein fragments were have been carried out. Therefore, we have carried out a theoretical structure-function analysis of all possible fragments of several meat and milk proteins in order to identify their primary structure regions that could serve as potential sources of regulatory oligopeptides and to reveal their possible previously unknown functions. The analysis was performed by comparing the primary structures of all possible bovine hemoglobin, cytochrome b, casein, α-lactalbumin, β-lactoglobulin, and lactoferrin fragments with the amino acid sequences of presently known natural regulatory oligopeptides. The oligopeptide structures were extracted from the EROP-Moscow database, contained data on the structures and functions of more than 9000 natural oligopeptides. The structure-function analysis revealed that a lot of different di-, tri-, and tetrapeptide protein fragments were precise copies of known regulatory oligopeptides obtained from members of all biological kingdoms. Functional analysis of these natural non-meat/milk oligopeptides has shown that they exhibited a broad spectrum of functional activities, such as neuropeptide, hormone, enzyme inhibitor, transporter, etc. The new terms fragmentomics and fragmentome were grounded and defined and practical applications of food protein fragments was considered on the basis of these results." @default.
- W362401545 created "2016-06-24" @default.
- W362401545 creator A5074895787 @default.
- W362401545 date "2009-08-20" @default.
- W362401545 modified "2023-09-23" @default.
- W362401545 title "Fragmentomics: a new insight into structures and functions of the natural oligopeptide diversity" @default.
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