Pérez M D, Calvo M
Tecnología y Bioquímica de los Alimentos, Facultad de Veterinaria, Zaragoza, Spain.
J Dairy Sci. 1995 May;78(5):978-88. doi: 10.3168/jds.S0022-0302(95)76713-3.
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.
β-乳球蛋白是反刍动物以及一些非反刍动物（如猪和马）乳汁中的主要乳清蛋白。尽管β-乳球蛋白于60年前首次被分离出来，但尚未明确其具体功能。最近的X射线晶体学研究增进了我们对β-乳球蛋白结构的了解，它与视黄醇结合蛋白和脂质运载蛋白具有同源性；这些蛋白质的功能似乎是参与小的疏水性物质的运输。由此类推，有人认为这种蛋白质可能具有脂肪酸和视黄醇转运蛋白的作用。鉴于过去几年积累的大量信息，本综述重新评估了β-乳球蛋白的功能。特别是，本综述重点关注视黄醇和脂肪酸与β-乳球蛋白结合的研究，包括结合常数和结合位点数量、结合位点的位置，以及蛋白质与两种配体相互作用时化学修饰的影响。本研究还描述了β-乳球蛋白对几个可能与其潜在生物学作用相关的生物学过程影响的研究。
