从黄瓜幼苗中分离出的碱性蓝蛋白的氨基酸序列。
Amino acid sequence of a basic blue protein from cucumber seedlings.
机构信息
Department of Inorganic Chemistry, The University of Sydney, New South Wales 2006, Australia.
出版信息
Proc Natl Acad Sci U S A. 1982 Nov;79(21):6434-7. doi: 10.1073/pnas.79.21.6434.
Abstract
The amino acid sequence of a type 1 copper protein, the 96-residue basic blue protein from cucumber seedlings, has been determined by Edman degradation of the intact molecule and of fragments produced by cleavage with cyanogen bromide and with trypsin. The cucumber basic blue protein shows a marked sequence homology with stellacyanin, and to a smaller degree with plastocyanin and azurin. The known copper ligands of plastocyanin and azurin (corresponding to histidine-37, cysteine-84, histidine-87, and methionine-92 in plastocyanin) are present in the cucumber basic blue protein. However, the latter also contains a half-cystine residue analogous to the suggested fourth ligand of stellacyanin, where methionine is absent.
摘要
已通过对完整分子及其用溴化氰和胰蛋白酶切割产生的片段进行 Edman 降解，确定了 1 型铜蛋白（来自黄瓜幼苗的 96 个残基碱性蓝蛋白）的氨基酸序列。黄瓜碱性蓝蛋白与星型细胞色素显示出明显的序列同源性，与质体蓝蛋白和细胞色素 c 较小程度的同源性。质体蓝蛋白和细胞色素 c 的已知铜配体（对应于质体蓝蛋白中的组氨酸-37、半胱氨酸-84、组氨酸-87 和蛋氨酸-92）存在于黄瓜碱性蓝蛋白中。然而，后者还含有一个半胱氨酸残基，类似于星型细胞色素的第四个配体的建议，其中蛋氨酸不存在。
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