AgResearch Ltd., Lincoln, New Zealand.
Adv Exp Med Biol. 2018;1054:173-183. doi: 10.1007/978-981-10-8195-8_12.
Trichocyte keratins differ considerably from their epithelial cousins in having a higher number of cysteine residues, of which the greater proportion are located in the head and tail regions of these proteins. Coupled with this is the presence of a large number of keratin associated proteins in these fibres that are high in their cysteine content, the high sulfur proteins and ultra-high sulfur proteins. Thus it is the crosslinking that occurs between the cysteines in the keratins and KAPs that is an important determinant in the functionality of wool and hair fibres. Studies have shown the majority of the cysteine residues are involved in internal crosslinking in the KAPs leaving only a few specific cysteines to interact with the keratins, with most evidence pointing to interactions between these KAP cysteines and the keratin head groups.
发状纤维角蛋白的半胱氨酸残基数量明显多于上皮角蛋白，其中大部分位于这些蛋白质的头部和尾部。此外，这些纤维中还存在大量富含半胱氨酸的角蛋白相关蛋白，即高硫蛋白和超高硫蛋白。因此，角蛋白和 KAP 之间的半胱氨酸交联是羊毛和毛发纤维功能的重要决定因素。研究表明，大多数半胱氨酸残基参与 KAP 中的内部交联，仅留下少数特定的半胱氨酸与角蛋白相互作用，大多数证据表明这些 KAP 半胱氨酸与角蛋白头部基团之间存在相互作用。
