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Secretory proteins as potential semiochemical carriers in the horse

机译：分泌蛋白作为马中潜在的化学信息载体

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摘要

Two soluble proteins were isolated as major secretory products of horse sweat and of the parotid gland and characterized for structural and functional properties. The first protein, lipocalin allergen EquC1, was characterized for its glycosylation sites and bound glycosidic moieties. Only one (Asn53) of the two putative glycosylation sites within the sequence was post-translationally modified; a different glycosylation pattern was determined with respect to data previously reported. When purified from horse sweat, this protein contained oleamide and other organic molecules as natural ligands. Ligand binding experiments indicated good protein selectivity toward volatile compounds having a straight chain structure of 9-11 carbon atoms, suggesting a role of this lipocalin in chemical communication. The second protein, here reported for the first time in the horse, belongs to the group of parotid secretory proteins, part of a large superfamily of binding proteins whose function in most cases is still unclear. This protein was sequenced and characterized for its post-translational modifications. Of the three cysteine residues present, two were involved in a disulfide bridge (Cys155-Cys198). A model, built up on the basis of similar proteins, indicated a general fold characterized by the presence of a long hydrophobic barrel. Binding experiments performed with a number of different organic compounds failed to identify ligands for this protein with a well-defined physiological role.
机译：分离出两种可溶性蛋白作为马汗和腮腺的主要分泌产物，并对其结构和功能特性进行了表征。第一个蛋白质，lipocalin过敏原EquC1，具有糖基化位点和结合的糖苷部分的特征。序列中两个推定糖基化位点中只有一个（Asn53）进行了翻译后修饰。对于先前报道的数据，确定了不同的糖基化模式。从马汗中提纯后，该蛋白质包含油酰胺和其他有机分子作为天然配体。配体结合实验表明，蛋白质对具有9-11个碳原子直链结构的挥发性化合物具有良好的蛋白质选择性，表明该脂笼蛋白在化学通讯中的作用。第二种蛋白质，是首次在马中报道的蛋白质，属于腮腺分泌蛋白，是腮腺结合蛋白超家族的一部分，在大多数情况下其功能尚不清楚。对该蛋白质进行测序，并对其翻译后修饰进行表征。在存在的三个半胱氨酸残基中，有两个与二硫键有关（Cys155-Cys198）。建立在相似蛋白质基础上的模型显示出以长疏水桶为特征的一般折叠。用多种不同的有机化合物进行的结合实验未能鉴定出具有明确定义的生理作用的该蛋白质的配体。

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