STUDIES TOWARDS COMPLETE SEQUENCE DETERMINATION OF PROTEINS BY MASS-SPECTROMETRY - DERIVATION OF METHIONINE, CYSTEINE AND ARGININE CONTAINING PEPTIDES

STUDIES TOWARDS COMPLETE SEQUENCE DETERMINATION OF PROTEINS BY MASS-SPECTROMETRY - DERIVATION OF METHIONINE, CYSTEINE AND ARGININE CONTAINING PEPTIDES
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DOI:
10.1016/0006-291x(73)90535-4
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发表时间:
1973-01-01
影响因子:
3.1
通讯作者:
WILLIAMS, DH
WILLIAMS, DH
中科院分区:
生物学4区
文献类型:
--
作者:
MORRIS, HR;DICKINSON, RJ;WILLIAMS, DH

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一些蛋氨酸、嘧啶鸟氨酸和两种羧甲基半胱氨酸肽在乙酰化和过甲基化后,反应时间约为60秒,具有易于解释的质谱。使用这种方法,在所有情况下都可以防止“盐”形成。对于含有精氨酸的多肽,描述了在二羰基缩合和肼解反应中产生高收率所需衍生物的改进方法。特别是在后一种情况下,许多酸性肽现在已经衍生,没有广泛的肽键切割和它们的序列确定。
A number of methionine, pyrimidyl ornithine, and two carboxymethyl cysteine containing peptides have given easily interpretable mass spectra following acetylation, and permethylation using a reaction time of about 60 seconds. Using this procedure involatile “salt” formation was prevented in all cases. For arginine containing peptides, refined methods are described for producing high yields of the required derivative in both dicarbonyl condensation and hydrazinolysis reactions. In the latter case in particular, a number of acidic peptides have now been derivatised without extensive peptide bond cleavage and their sequences determined.