Isolation of the bombesin-immunoreactive peptide from bovine milk and its tentative identification as alpha-s1 casien 101–103

Ekeke, N.U.; Shaw, Chris; Johnston, C.F.; Thim, Lars; Love, A. H. G.

doi:10.1016/0167-0115(92)90198-4

Regulatory Peptides

1992

DOI: 10.1016/0167-0115(92)90198-4

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Isolation of the bombesin-immunoreactive peptide from bovine milk and its tentative identification as alpha-s1 casien 101–103

N.U. Ekeke¹,

Chris Shaw²,

C.F. Johnston³

et al.

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Fragmentomics of natural peptide structures

Zamyatnin

2009

Biochemistry Moscow

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Natural fragmentation of peptide and other chemical structures is well known. They are a significant object of biochemical investigations. In this connection, the bases and determination are given for the notion of the "fragmentome" as a set of all fragments of a single substance, as well as for global fragmentome of all chemical components of living organisms. It is described how protein-peptide fragments are formed in nature, what experimental and theoretical methods are used for their investigation, as well as mathematical characteristics of fragmentomes. Individual fragmentomes of all subunits and of complete casein fragmentome are considered in detail. Structural and functional variety of its possible fragments was revealed by computer analysis. Formation in an organism of an exogenous-endogenous pool of oligopeptides and correlation of these data with concepts of structure-functional continuum of regulatory molecules is shown on an example of food protein fragments. Possible practical importance of the use of natural fragments in dietology, therapy, as well as in sanitary hygiene and cosmetics is noted.

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Fragmentomics of natural peptide structures

Zamyatnin

2009

Biochemistry Moscow

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Food protein fragments are regulatory oligopeptides

Zamyatnin

Voronina

2012

Biochemistry Moscow

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Until recently food proteins were considered to be an energy source and a source of essential and nonessential amino acids required for protein synthesis and precursors of many vital biomolecules. However, we assumed earlier that food protein fragments might perform some regulatory functions. The theoretical justification for this assumption is advanced in this work. In the present work, the primary structures of protein fragments were compared with amino acid sequences of known natural regulatory oligopeptides in silico. It is shown that fragments formed as a result of animal food protein cleavage by proteolytic enzymes can exist in the gastrointestinal tract for a long time. Many of them are enzyme inhibitors, regulators of nervous, endocrine, and immune system, and possess antimicrobial and other activities. It has also been shown that the lifetime of fragments before their cleavage in the gastrointestinal tract could be enough for performing corrective functions. Thus, as a result of food protein fragmentation a dynamic pool of exogenous regulatory oligopeptides with functions changing as shorter fragments are generated may form. The detection of an endogenous-exogenous pool of regulatory molecules expands the significance and content of the Ashmarin-Obukhova hypothesis on a functional continuum of natural oligopeptides. The possible practical importance of these results is noted.

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Isolation of the bombesin-immunoreactive peptide from bovine milk and its tentative identification as alpha-s1 casien 101–103

Cited by 2 publications

References 0 publications

Fragmentomics of natural peptide structures

Fragmentomics of natural peptide structures

Food protein fragments are regulatory oligopeptides

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