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Folate binding proteins.

S Waxman

    British Journal of Haematology
    |January 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Fatty acid-binding proteins (FABP) are present in body fluids and tissues, influencing folate metabolism. These proteins, found in serum, milk, and cells, play a significant role in this metabolic pathway.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Physiology

    Background:

    • Fatty acid-binding proteins (FABP) are a family of intracellular proteins known for their role in lipid metabolism.
    • FABPs are involved in the transport and metabolism of fatty acids and other hydrophobic molecules.
    • Previous research has indicated the presence of FABPs in various biological matrices.

    Purpose of the Study:

    • To present the physical and physiologic properties of serum, milk, and cellular Fatty Acid-Binding Proteins (FABP).
    • To establish the widespread presence and characteristics of FABP across different body fluids and tissues.
    • To elucidate the potential role of FABP in influencing folate metabolism.

    Main Methods:

    • Review and presentation of existing data on the physical and physiologic properties of FABP from serum, milk, and cellular sources.

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  • Compilation of evidence from multiple investigators regarding the presence and characteristics of FABP in various body fluids and tissues.
  • Analysis of the established role of FABP in biological systems.

    • Main Results:

    • The physical and physiologic properties of serum, milk, and cellular FABP have been characterized.
    • FABP with consistent characteristics has been identified in diverse body fluids and tissues.
    • Evidence suggests FABP is a significant factor in folate metabolism.

    Conclusions:

    • Fatty Acid-Binding Proteins (FABP) exhibit conserved properties across serum, milk, and cellular compartments.
    • The ubiquitous presence of FABP in body fluids and tissues underscores its systemic importance.
    • FABP is established as a key protein influencing the complex process of folate metabolism.