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1
Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment.来自S-羧甲基角蛋白-A的α-螺旋片段的氨基酸序列。II型片段的完整序列。
Biochem J. 1978 Aug 1;173(2):365-71. doi: 10.1042/bj1730365.
2
Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Tryptic and chymotryptic peptides from a type-II segment.来自S-羧甲基角蛋白-A的α-螺旋片段的氨基酸序列。来自II型片段的胰蛋白酶和胰凝乳蛋白酶肽段。
Biochem J. 1978 Aug 1;173(2):353-63. doi: 10.1042/bj1730353.
3
Amino acid sequences of alpha-helical segments from S-carbosymethylkerateine-A. Complete sequence of a type-I segment.来自S-羧甲基角蛋白A的α-螺旋片段的氨基酸序列。I型片段的完整序列。
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4
Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Statistical analysis.来自S-羧甲基角蛋白A的α-螺旋片段的氨基酸序列。统计分析。
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The primary structure of component 8c-1, a subunit protein of intermediate filaments in wool keratin. Relationships with proteins from other intermediate filaments.羊毛角蛋白中间丝亚基蛋白8c-1的一级结构。与其他中间丝蛋白的关系。
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The amino acid sequence of protein SCMK-B2A from the high-sulphur fraction of wool keratin.羊毛角蛋白高硫组分中蛋白质SCMK-B2A的氨基酸序列。
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Evidence of homology in a high-sulphur protein fraction (SCMK-B2) of wool and hair alpha-keratins.羊毛和毛发α-角蛋白的高硫蛋白质组分（SCMK-B2）中同源性的证据。
Biochem J. 1968 Nov;110(2):193-200. doi: 10.1042/bj1100193.

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1
Structures of the ß-Keratin Filaments and Keratin Intermediate Filaments in the Epidermal Appendages of Birds and Reptiles (Sauropsids).鸟类和爬行类（蜥臀目）表皮附属物中的β-角蛋白丝和角蛋白中间丝的结构。
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Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin.通过氨基酸序列分析比较两种免疫特性不同的中间丝蛋白：结蛋白和波形蛋白。
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Intermediate filaments of baby hamster kidney (BHK-21) cells and bovine epidermal keratinocytes have similar ultrastructures and subunit domain structures.幼仓鼠肾（BHK - 21）细胞和牛表皮角质形成细胞的中间丝具有相似的超微结构和亚基结构域结构。
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Molecular cloning and primary structure of human glial fibrillary acidic protein.人胶质纤维酸性蛋白的分子克隆与一级结构
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Concerted gene duplications in the two keratin gene families.
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本文引用的文献

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The isomeric transformation of urea into ammonium cyanate in aqueous solutions.尿素在水溶液中异构转化为氰酸铵。
Biochem J. 1948;42(4):628-32.
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A protein sequenator.蛋白质测序仪。
Eur J Biochem. 1967 Mar;1(1):80-91. doi: 10.1007/978-3-662-25813-2_14.
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X-ray diffraction and infrared studies of an -helical fragment from -keratin.
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Fourteen actin-binding sites on tropomyosin?原肌球蛋白上有14个肌动蛋白结合位点？
Nature. 1975 Sep 25;257(5524):331-3. doi: 10.1038/257331a0.
7
Determination of the amino acid sequence of apovitellenin I from duck's egg yolk using an improved sequenator procedure: a comparison with other avian species.
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8
Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Tryptic and chymotryptic peptides from a type-II segment.来自S-羧甲基角蛋白-A的α-螺旋片段的氨基酸序列。来自II型片段的胰蛋白酶和胰凝乳蛋白酶肽段。
Biochem J. 1978 Aug 1;173(2):353-63. doi: 10.1042/bj1730353.

来自S-羧甲基角蛋白-A的α-螺旋片段的氨基酸序列。II型片段的完整序列。

Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment.

作者信息

Crewther W G, Inglis A S, McKern N M

出版信息

Biochem J. 1978 Aug 1;173(2):365-71. doi: 10.1042/bj1730365.

DOI:10.1042/bj1730365
PMID:581264
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1185788/
Abstract
  1. The helical fragments obtained by partial chymotryptic digestion of S-carboxymethylkeratine-A, the low-sulphur fraction from wool, were fractionated into type-I and type-II helical segments in aqueous urea under conditions limiting carbamoylation. 2. The amino acid sequence of a 109-residue type-II segment was completed by using the sequenator. 3. When the data were incorporated into a helical model of 3.6 residues per turn the hydrophobic residues generated a band aligned at a slight angle to the helical axis. This result is in accord with the postulated coiled-coil structure of the crystalline regions of alpha-keratin.
摘要
  1. 通过对羊毛中的低硫组分S-羧甲基角蛋白-A进行部分胰凝乳蛋白酶消化得到的螺旋片段，在限制氨甲酰化的条件下，于尿素水溶液中被分离为I型和II型螺旋片段。2. 使用序列分析仪完成了一个109个残基的II型片段的氨基酸序列测定。3. 当将这些数据纳入每圈3.6个残基的螺旋模型时，疏水残基形成了一条与螺旋轴成小角度排列的带。这一结果与α-角蛋白晶体区域的假定卷曲螺旋结构一致。