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从黑天鹅蛋清中分离出一种碱性低分子量蛋白质并测定其完整氨基酸序列。

Isolation and complete amino acid sequence of a basic low molecular weight protein from black swan egg white.

作者信息

Simpson R J, Morgan F J

出版信息

Int J Pept Protein Res. 1983 Oct;22(4):476-81.

PMID:6654595
Abstract

The following complete amino acid sequence of a low molecular weight basic protein (Mr 4,454) from black swan egg white has been determined: less than Glu-Val-Arg-Lys-Tyr-Cys-Pro-Lys-Val-Gly-Tyr-Cys-Ser-Ser-Lys-Cys-Ser-Lys-Ala-Asp-Val-Trp-Ser-Leu-Ser-Ser-Asp-Cys-Lys-Phe-Tyr-Cys-Cys-Leu-Pro-Pro-Gly-Trp-Lys. There is significant homology between this protein, provisionally designated cygnin, and the NH2-terminal region of the second domain of chicken ovotransferrin. The disulfide bonds have not been assigned; however, the arrangement of half-cystines in cygnin is sufficiently different from that of the known transferrins to suggest that cygnin is derived from another gene.

摘要

已测定了来自黑天鹅蛋清的一种低分子量碱性蛋白(分子量4454)的完整氨基酸序列:Glu-Val-Arg-Lys-Tyr-Cys-Pro-Lys-Val-Gly-Tyr-Cys-Ser-Ser-Lys-Cys-Ser-Lys-Ala-Asp-Val-Trp-Ser-Leu-Ser-Ser-Asp-Cys-Lys-Phe-Tyr-Cys-Cys-Leu-Pro-Pro-Gly-Trp-Lys及以下部分。该蛋白暂命名为天鹅蛋白,与鸡卵转铁蛋白第二个结构域的氨基末端区域存在显著同源性。尚未确定二硫键;然而,天鹅蛋白中半胱氨酸的排列与已知转铁蛋白的排列有足够差异,表明天鹅蛋白源自另一个基因。

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