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Proteolytic Processing of Histone H2A by the Cathepsin L protease

机译:组织蛋白酶L蛋白酶组蛋白H2A的蛋白水解加工

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The ETD-MS/MS data showed an abundant cleavage after amino acid 44. The motif being clipped is YAERVG-AGAPV. After this cleavage, a 9228.20502 Da N-terminal polypeptide is generated, and opposite to the intact protein, the abundance of this peptide increases over time. Analysis of the digested samples by SDS gel confirmed that Cathepsin L is able to digest H2A in-vitro. After one hour, the amount of intact histone drastically decreased compared to the input.
机译:ETD-MS / MS数据在氨基酸44后显示出充分的裂解。被剪裁的基序是Yaervg-Agapv。在该切割后,产生9228.20502Da n末端多肽,并且与完整蛋白质相反,该肽的丰度随时间增加。通过SDS凝胶分析消化的样品证实,组织蛋白酶L能够在体外消化H2A。一个小时后,与输入相比,完整组蛋白的量大幅下降。

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