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Journal of dairy science1995; 78(5); 978-988; doi: 10.3168/jds.S0022-0302(95)76713-3

Interaction of beta-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review.

Abstract: beta-Lactoglobulin is the major whey protein in the milk of ruminants and some nonruminants, such as pigs and horses. Although beta-lactoglobulin was first isolated 60 yr ago, no function has been definitely ascribed to beta-lactoglobulin. Recent x-ray crystallographic studies have advanced knowledge of the structure of beta-lactoglobulin, which is homologous with that of retinol-binding protein and lipocalycins; the function of these proteins seems to be participation in the transport of small hydrophobic substances. By analogy, this protein has been suggested as having a role as a transporter of fatty acids and retinol. This review reassesses the function of beta-lactoglobulin in light of the large amount of information that has accrued in the last few years. In particular, this review concentrates upon studies of the binding of retinol and fatty acids to beta-lactoglobulin, including the binding constants and number of binding sites, the location of the binding sites, and the influence of chemical modifications in the interaction of the protein with both ligands. This study also describes studies of the influence of beta-lactoglobulin on several biological processes that may be relevant to the possible biological role of this protein.
Publication Date: 1995-05-01 PubMed ID: 7622732DOI: 10.3168/jds.S0022-0302(95)76713-3Google Scholar: Lookup
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  • Journal Article
  • Review

Summary

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This research study reviews the role of beta-lactoglobulin, a major whey protein found in ruminants’ milk and some non-ruminants like pigs and horses. It explores the protein’s potential function as a transporter of retinol and fatty acids, focusing on how it binds with these substances and its possible influence on biological processes.

Background on Beta-Lactoglobulin

  • Beta-lactoglobulin is a significant whey protein found in ruminants’ milk, such as cows, and some non-ruminants, like pigs and horses.
  • Despite its discovery over six decades ago, there is still no definitive function assigned to this protein, making it an active subject of study in the scientific community.
  • The structure of beta-lactoglobulin, as revealed through recent x-ray crystallographic studies, correlates with that of retinol-binding protein and lipocalycins, giving rise to hypotheses about its purpose.

Function as a Transporter of Retinol and Fatty Acids

  • Considering its structural similarity with other proteins like retinol-binding protein and lipocalycins, beta-lactoglobulin is believed to have a role as a transporter of smaller hydrophobic substances.
  • Through this analogy, researchers propose that beta-lactoglobulin might contribute to the transportation of retinol and fatty acids.
  • This review reassesses this potential role of beta-lactoglobulin as a transporter by compiling and examining the vast amount of information obtained over the past few years.

Binding of Retinol and Fatty Acids to Beta-Lactoglobulin

  • One critical focus of the review is to study the relation of beta-lactoglobulin with retinol and fatty acids, particularly in how it attaches to these substances.
  • It analyses the binding constants and the number of binding sites, as well as the physical locations of these binding sites on the protein molecule.
  • The review further examines how chemical modifications can alter the interaction of the protein with both ligands.

Impact on Biological Processes

  • Apart from being a possible transporter, this review explores how beta-lactoglobulin might influence various biological processes.
  • These potential influences could offer more insights into the biological role of this protein, further enhancing our understanding of its functions within the body.

Cite This Article

APA
Pérez MD, Calvo M. (1995). Interaction of beta-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. J Dairy Sci, 78(5), 978-988. https://doi.org/10.3168/jds.S0022-0302(95)76713-3

Publication

ISSN: 0022-0302
NlmUniqueID: 2985126R
Country: United States
Language: English
Volume: 78
Issue: 5
Pages: 978-988

Researcher Affiliations

Pérez, M D
  • Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Zaragoza, Spain.
Calvo, M

    MeSH Terms

    • Animals
    • Fatty Acids / metabolism
    • Lactoglobulins / physiology
    • Ruminants
    • Vitamin A / metabolism

    Citations

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