ISOLATION AND CHARACTERIZATION OF LATHERIN, A SURFACE-ACTIVE PROTEIN FROM HORSE SWEAT
ISOLATION AND CHARACTERIZATION OF LATHERIN, A SURFACE-ACTIVE PROTEIN FROM HORSE SWEAT
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DOI：
10.1042/bj2350645
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发表时间：
1986-05-01
影响因子：
4.1
通讯作者：
SNOW, DH
中科院分区：
文献类型：
--
作者：
BEELEY, JG;EASON, R;SNOW, DH
通过凝胶过滤和离子交换层析从马汗中分离得到一种具有特殊表面活性的蛋白质--泡沫蛋白。该蛋白质的斯托克斯半径（通过凝胶过滤测定）为2.47 nm，在超浓缩沉积物中为单一物种，s20，w 2.05 S，表明Mr为24，400。在SDS/聚丙烯酰胺凝胶电泳上，该分子表现为表观Mr 20，000的单链肽链。泡沫蛋白含有高比例的疏水性氨基酸（37.2%），并且亮氨酸含量（24.5%）异常高。蛋白质的不寻常的组合物可以解释明显的异常，在由经验方法确定的兰瑟素的先生。通过表面张力的简单测定和接触角测量，获得了表明起泡剂是马汗的大部分表面活性的原因的证据。泡沫蛋白非常容易吸附在疏水表面上，使其呈亲水性。一个可能的作用，泡沫蛋白在体温调节的建议。
A protein, latherin, with unusual surface activity was isolated from horse sweat by gel filtration and ion-exchange chromatography. The protein has a Stokes radius, determined by gel filtration, of 2.47 nm, and in the ultracentrifuge sediments as a single species with s20,w 2.05 S, indicating an Mr of 24,400. On SDS/polyacrylamide-gel electrophoresis the molecule behaves as a single peptide chain of apparent Mr 20,000. Latherin contains a high proportion of hydrophobic amino acids (37.2%), and the leucine content (24.5%) is exceptionally high. The unusual composition of the protein may account for apparent anomalies in the Mr of lantherin determined by empirical methods. Evidence indicating that latherin is responsible for much of the surface activity of horse sweat was obtained by a simple assay for surface tension and by contact-angle measurements. Latherin adsorbs very readily at hydrophobic surfaces, rendering them wettable. A possible role for latherin in thermoregulation is proposed.