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首页> 外文期刊>Journal of Protein Chemistry >Cleavage specificities of individual members of kallikrein family of proteins on synthetic peptide containing the bradykinin sequence.
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Cleavage specificities of individual members of kallikrein family of proteins on synthetic peptide containing the bradykinin sequence.

机译:激肽释放酶家族蛋白的单个成员在含有缓激肽序列的合成肽上的切割特异性。

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摘要

We have analyzed the effect on bond specificity of various isolated members of the mouse kallikrein family of proteins on a synthetic peptide containing the bradykinin sequence. The cleavage pattern shows the selected specificity of these proteases toward the synthetic peptide. The Phe-His bond (positions 11-12) in the synthetic peptide was favorably cleaved by most of the members in this family, including gamma nerve growth factor. On the other hand, the Lys-Arg bond (position 3-4) was found to be susceptible only to gamma-NGF. The combination of these cleavages could result in the degradation of bradykinin in vivo.
机译:我们已经分析了小鼠激肽释放酶家族蛋白的各种分离成员对含有缓激肽序列的合成肽的键特异性的影响。切割模式显示了这些蛋白酶对合成肽的选定特异性。合成肽中的Phe-His键(11-12位)被该家族的大多数成员(包括γ神经生长因子)有利地裂解。另一方面,发现Lys-Arg键(3-4位)仅对γ-NGF敏感。这些切割的结合可导致缓激肽在体内的降解。

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