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Biokhimiia (Moscow, Russia)1976; 41(7); 1285-1290;

[Equine pepsins].

Abstract: 6 forms of pepsin are found in horse gastric juice. Amino acid sequence is determined of N-terminal (most variable) part of polypeptide chain of main pepsin components. Equine pepsines, which have pI 2.1 and 2.3, are found to have identical amino acid sequence at least for 31 amino acid residues. The same sequence is observed in the component with pI 2.6 for 10 first residues. The sequence of equine pepsin with pI 3.2 has 3 substitutions for 33 amino acids, when compared with pepsines having pI 2.1 and 2.3. The forms of equine pepsin studied are more similar than the other isoenzyme pair, human pepsin and gastricsin.
Publication Date: 1976-01-01 PubMed ID: 793642
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Summary

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The research article describes a study on the characteristics and variations of the enzyme pepsin in horse gastric juice, confirming the existence of six different forms, their similar and differing amino acid sequences, and the comparison of equine pepsins to human enzyme counterparts.

Study on Equine Pepsins

  • The primary objective of the research was to discover and analyze the properties of different forms of pepsin present in horse gastric juice, to better understand biological processes and enzymatic functionality in horses, and to compare these with analogous enzymes in humans.
  • Peptin is an enzyme that breaks down proteins into smaller peptides. The details of enzymes in animals, like their variations, characteristics, and sequence of compounds, are essential for understanding animal biology and medical research.

Determination of Amino Acid Sequences

  • The research focused on understanding the variable part of the polypeptide chains, more specifically on the N-terminal part. This determination of sequences was important as the unique arrangement and ordering of the sequence contributes to its specific interactive properties and functions within the horse’s body.
  • The study reported that certain equine pepsins exhibited identical amino acid sequences for a certain number of residues.

Analysis of pIValue

  • The study also analyzed the enzymatic differences and similarities based on their pI (isoelectric point) values. The isoelectric point is the pH at which a particular molecule carries no net electrical charge.
  • The pepsins, regulated by pI values of 2.1, 2.3, and 2.6 showed varying levels of sequence similarity. The equine pepsin with a pI value of 3.2 exhibited three substitutions for 33 amino acids when compared with pepsins having pI 2.1 and 2.3.

Comparison with Human Isoenzyme Pairs

  • The research concluded by drawing a comparative analysis between the different forms of equine pepsins and the corresponding human isoenzymes — pepsin and gastricsin. According to the findings, equine pepsin forms studied exhibited more similarity to each other than human pepsin and gastricsin, indicating lesser variability in the horse’s gastric enzymes, and potentially pointing to differences in human and equine digestive processes.

Cite This Article

APA
Stepanov VM, Lavrenova GI, Rudenskaia GN, Gonchar MV, Lebareva LS. (1976). [Equine pepsins]. Biokhimiia, 41(7), 1285-1290.

Publication

ISSN: 0320-9725
NlmUniqueID: 0372667
Country: Russia (Federation)
Language: rus
Volume: 41
Issue: 7
Pages: 1285-1290

Researcher Affiliations

Stepanov, V M
    Lavrenova, G I
      Rudenskaia, G N
        Gonchar, M V
          Lebareva, L S

            MeSH Terms

            • Amino Acid Sequence
            • Animals
            • Chemical Phenomena
            • Chemistry
            • Gastric Juice / enzymology
            • Horses
            • Isoelectric Point
            • Isoenzymes
            • Pepsin A / isolation & purification
            • Phosphorus

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