Abstract
This article continues a series of reviews about the structure and functions of milk fat globule membrane (MFGM) proteins in cow’s milk. This installment introduces publications on the biochemistry of fatty acid binding protein (FABP), which is a polypeptide component of MFGM. The article gives a brief history of its discovery, as well as profiles the proteins that bind hydrophobic ligands and describes the methods of FABP identification in MFGM preparations. Other aspects of FABP studies include: isoforms and modern nomenclature; amino acid sequence and reactions to post-translational modification; spatial organization; mechanisms for binding fatty acids to lipids; well-investigated and hypothesized physiological functions; the effect of haplotypes on milk fatty acids, yield, and protein content.
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