Steinert P M, Peck G L, Idler W W
Curr Probl Dermatol. 1980;10:391-406. doi: 10.1159/000396303.
The chemistry and structure of the epidermal alpha-keratin extracted from the skin of patients with a variety of disorders of keratinization have been investigated using biochemical, biophysical, and electron microscopic techniques developed for the characterization of normal mammalian epidermal keratin. Generally, the alpha-keratin polypeptides of the diseased epidermis differed from those of uninvolved epidermis or of normal volunteers in having varying numbers of polypeptide components of lower molecular weights, numerous free amino acids, higher contents of alpha-helix, and only limited facility for polymerization in vitro into native-type epidermal keratin filaments. As the alpha-helix-enriched fragments, which represent up to two-thirds of the polypeptide chains, isolated after limited tryptic digestion of the keratin filaments of normal, uninvolved, and involved epidermis, were physicochemically identical, it seems that the end-terminal non-alpha-helical regions of the polypeptides of diseased epidermis are abnormal. These differences may be a result of degradation or of altered protein synthesis.
利用为鉴定正常哺乳动物表皮角蛋白而开发的生化、生物物理和电子显微镜技术，对从患有各种角化异常疾病患者皮肤中提取的表皮α-角蛋白的化学性质和结构进行了研究。一般来说，患病表皮的α-角蛋白多肽与未受累表皮或正常志愿者的α-角蛋白多肽不同，其低分子量多肽成分数量不同、有大量游离氨基酸、α-螺旋含量更高，并且在体外聚合成天然型表皮角蛋白丝的能力有限。由于在对正常、未受累和受累表皮的角蛋白丝进行有限胰蛋白酶消化后分离出的富含α-螺旋的片段（占多肽链的三分之二）在物理化学性质上是相同的，所以患病表皮多肽的末端非α-螺旋区域似乎是异常的。这些差异可能是降解或蛋白质合成改变的结果。
