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Biochimica et biophysica acta1986; 874(1); 54-60; doi: 10.1016/0167-4838(86)90101-9

Spectrofluorimetric study of the bile salt micelle binding site of pig and horse colipases.

Abstract: Pig and horse colipases contain three tyrosine residues. In addition, horse colipase possesses a tryptophan residue. Some of the tyrosine residues are involved in the association of colipase and a bile salt micelle. The present report demonstrates that the aromatic residues responsible for colipase fluorescence are in an aqueous environment. In the presence of bile salt micelles, changes in colipase fluorescence properties indicate that the intrinsic fluorophores are located in a more hydrophobic environment upon colipase-micelle complex formation. In addition, the fluorescence of an NBD group fixed on lysine 60, which is very close to the aromatic region in the pig colipase, is also altered in the presence of micelles. These results show that the micelle binding site is not limited to the tyrosine residues but may be broadened to adjacent residues such as lysine 60 and also tryptophan 52 in horse colipase.
Publication Date: 1986-11-07 PubMed ID: 3768376DOI: 10.1016/0167-4838(86)90101-9Google Scholar: Lookup
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Summary

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The study explores how the tyrosine residues in pig and horse colipases interact with bile salt micelles—tiny particles that aid in fat digestion. The research showed that these aromatic residues providing the colipase’s fluorescence are in an aqueous environment and their fluorescence properties change when the colipase binds with the bile salt micelle, indicating a more hydrophic environment.

Purpose and Scope of the Research

  • The primary aim of the research was to elucidate the interaction of bile salt micelles with colipases, proteins that act as cofactors in the hydrolysis of dietary fat.
  • The researchers focused specifically on the role of three tyrosine residues found in pig and horse colipases.
  • The study also explored the effects of a tryptophan residue, only present in horse colipase, on this interaction.

Key Findings

  • The researchers found that some of the tyrosine residues are integral to the binding of colipase and bile salt micelles.
  • They also discovered that the fluorescence of colipase, which is derived from the aromatic residues such as tyrosine, are surrounded by water elements. Upon binding with the micelle, these residues become part of a more lipid-like environment, as evident from the change in their fluorescence properties.
  • The study revealed that the fluorescence of a nitrobenzoxadiazole (NBD) group attached to lysine 60, a region close to the aromatic zone in pig colipase, changes in the presence of micelles. This observation led to the conclusion that the micelle binding zone may extend further than just the tyrosine residues.
  • The researchers also hypothesized that adjacent residues, like lysine 60 and tryptophan 52 (in horse colipase), could be involved in the bile salt micelle binding process.

Implications of the Research

  • These findings broaden the context of understanding the molecular interactions between colipases and bile salt micelles.
  • This research could pave the way for future studies aimed at enhancing the bioavailability of hydrophobic drugs or improving fat digestion treatments.

Cite This Article

APA
Granon S. (1986). Spectrofluorimetric study of the bile salt micelle binding site of pig and horse colipases. Biochim Biophys Acta, 874(1), 54-60. https://doi.org/10.1016/0167-4838(86)90101-9

Publication

ISSN: 0006-3002
NlmUniqueID: 0217513
Country: Netherlands
Language: English
Volume: 874
Issue: 1
Pages: 54-60

Researcher Affiliations

Granon, S

    MeSH Terms

    • Animals
    • Bile Acids and Salts / metabolism
    • Binding Sites
    • Colipases / analysis
    • Horses
    • Micelles
    • Proteins / analysis
    • Spectrometry, Fluorescence
    • Swine
    • Tryptophan / analysis
    • Tyrosine / analysis

    Citations

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