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在一种显性遗传的外胚层发育异常中一组同源蛋白质的缺失。

Loss of a homologous group of proteins in a dominantly inherited ectodermal malformation.

作者信息

Tenenhouse H S, Gold R J

出版信息

Biochem J. 1976 Oct 1;159(1):149-57. doi: 10.1042/bj1590149.

DOI:10.1042/bj1590149
PMID:1036688
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1164047/
Abstract

Hair from mice bearing the dominantly inherited Naked trait (NN) and from normal (NN) mice of the same inbred strain was separated into its major protein components by standard techniques. The relative amounts of proteins in these components were then determined by a regression method from the amino acid composition of the hair samples and of the fractions into which they had been separated. The results indicated that the amount of soluble fibril in Naked-mouse hair is decreased. Polyacrylamide-gel electrophoresis of this fraction prepared from the hair of both normal and Naked mice revealed that all protein bands present in the normal are also present in the Naked mice. However, a densitometric scan of the gels at 280 nm showed that the soluble fibril fraction from Naked-mouse hair is deficient in several proteins which, on amino acid analysis, were found to contain 31% glycine and 10% tyrosine. Gel filtration of S-carboxymethylkerateine prepared from normal and mutant hair showed that the mutant hair is deficient in a heterogeneous, low-molecular-weight fraction also rich in glycine and tyrosine. Our present data do not reveal the mechanism whereby a single gene locus modulates the production of several different proteins.

摘要

采用标准技术将携带显性遗传无毛性状(NN)的小鼠以及同一近交系正常(NN)小鼠的毛发分离成主要蛋白质成分。然后,根据毛发样本及其分离所得组分的氨基酸组成,通过回归方法确定这些组分中蛋白质的相对含量。结果表明,无毛小鼠毛发中可溶性纤维的含量降低。对正常小鼠和无毛小鼠毛发制备的该组分进行聚丙烯酰胺凝胶电泳显示,正常小鼠毛发中存在的所有蛋白条带在无毛小鼠中也都存在。然而,在280nm处对凝胶进行光密度扫描显示,无毛小鼠毛发的可溶性纤维组分中几种蛋白质含量不足,经氨基酸分析发现这些蛋白质含有31%的甘氨酸和10%的酪氨酸。对正常毛发和突变毛发制备的S - 羧甲基角蛋白进行凝胶过滤显示,突变毛发缺乏一种同样富含甘氨酸和酪氨酸的异质性低分子量组分。我们目前的数据并未揭示单个基因座调节几种不同蛋白质产生的机制。

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Loss of a homologous group of proteins in a dominantly inherited ectodermal malformation.在一种显性遗传的外胚层发育异常中一组同源蛋白质的缺失。
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引用本文的文献

1
A method for calculating the relative protein contents of the major keratin components from their amino acid composition.一种根据主要角蛋白成分的氨基酸组成计算其相对蛋白质含量的方法。
Biochem J. 1976 Oct 1;159(1):157-60. doi: 10.1042/bj1590157.

本文引用的文献

1
DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.圆盘电泳。II. 方法及其在人血清蛋白中的应用。
Ann N Y Acad Sci. 1964 Dec 28;121:404-27. doi: 10.1111/j.1749-6632.1964.tb14213.x.
2
The characterization of hereditary abnormalities of keratin: Clouston's ectodermal dysplasia.
Birth Defects Orig Artic Ser. 1971 Jun;7(8):91-5.
3
Properties of hair keratin in an autosomal dominant form of ectodermal dysplasia.常染色体显性外胚层发育不良中毛发角蛋白的特性
Am J Hum Genet. 1972 Sep;24(5):549-61.
4
Proteins rich in glycine and tyrosine from keratins.
Comp Biochem Physiol B. 1972 Apr 15;41(4):723-34. doi: 10.1016/0305-0491(72)90085-5.
5
Tyrosine-rich proteins in keratins.
Comp Biochem Physiol B. 1973 Mar 15;44(3):943-7. doi: 10.1016/0305-0491(73)90244-7.
6
Biochemical marker in dominantly inherited ectodermal malformation.
Nature. 1974 Oct 4;251(5474):431-2. doi: 10.1038/251431a0.
7
Ninhydrin reactive contaminants from Dowex-50 cation exchange resins.
Anal Biochem. 1974 Nov;62(1):305-9. doi: 10.1016/0003-2697(74)90393-5.
8
A method for calculating the relative protein contents of the major keratin components from their amino acid composition.一种根据主要角蛋白成分的氨基酸组成计算其相对蛋白质含量的方法。
Biochem J. 1976 Oct 1;159(1):157-60. doi: 10.1042/bj1590157.