The effect of ferrimyoglobin on the oxidation of succinic acid by horse heart muscle preparations.
Abstract: In a series of model reactions, it is shown that residues
of ~-aminoacids may be inserted by a particular rearrangement into certain carboxyl or carbonylamido
groups. Repeated insertion results in the formation of
a peptide derivative. It is concluded that natural peptides or proteins must not necessarily be formed by head
to tail combination of aminoacids, Other implications of
the new principle are discussed.
Publication Date: 1955-10-15 PubMed ID: 13277463DOI: 10.1007/BF02158505Google Scholar: Lookup
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- Journal Article
Summary
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This research paper demonstrates that residues of amino acids can be added into select carboxyl or carbonylamido groups through a specific rearrangement process, which can result in the creation of a peptide derivative. The findings suggest that natural peptides or proteins don’t need to be formed by a sequential combination of amino acids.
Summary of the Research Article
- The research paper centers around a series of model reactions that illustrate how residues of amino acids could be incorporated into particular carboxyl or carbonylamido groups through a certain rearrangement process.
- The repeated insertion of residues in this way eventually led to the formation of a peptide derivative.
Significance of the Research Findings
- One significant finding from this research is the suggestion that natural peptides or proteins do not necessarily need to be created by a “head to tail” combination of amino acids.
- This new discovery challenges some existing conventional understanding of how peptides or proteins are formed and underscores the potential for other models of protein formation.
Additional Implications of the Research
- Further implications of this newly proposed principle were discussed in the paper, although they are not specified in the abstract.
- Given the fundamental role that peptides and proteins play in biological systems, these findings may have wide-ranging impacts on various fields such as synthetic biology, biochemistry, and pharmaceutical design.
Cite This Article
APA
AZZONE GF.
(1955).
The effect of ferrimyoglobin on the oxidation of succinic acid by horse heart muscle preparations.
Experientia, 11(10), 399-400.
https://doi.org/10.1007/BF02158505 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Hemoglobins
- Horses
- Humans
- Metmyoglobin
- Myocardium
- Oxidation-Reduction
- Succinates / metabolism
- Succinic Acid
References
This article includes 2 references
- DRABKIN DL. Spectrophotometric studies. XV. Hydration of macro sized crystals of human hemoglobin, and osmotic concentrations in red cells.. J Biol Chem 1950 Jul;185(1):231-45.
- Keilin D, Hartree EF. Activity of the cytochrome system in heart muscle preparations.. Biochem J 1947;41(4):500-2.
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