论文部分内容阅读
本文建立了运用毛细管电泳同时非放射分析蛋白质或多肽中的各种Ｏ－磷酸化氨基酸方法。将蛋白质或多肽部分水解成自由氨基酸，然后衍生为ＰＴＨ－氨基酸，再用毛细管电泳仪分离分析ＰＴＨ－磷酸化氨基酸。在２５至２５０ｐｍｏｌ／μｌ浓度范围内，３种Ｏ－磷酸化氨基酸的浓度对其衍生物ＵＶ吸光值的线性相关系数均大于０．９９２（ｎ＝６）。方法检测限在ｆｍｏｌ水平。运用该方法对３个模型磷酸化肽及天然的磷酸化蛋白β－酪蛋白和卵黄高磷蛋白的磷酸化位点进行了分析。
This paper established a method for the simultaneous non-radioactive analysis of various O-phosphorylated amino acids in proteins or peptides by capillary electrophoresis. The protein or polypeptide is partially hydrolyzed to free amino acids, then to PTH-amino acids, and the PTH-phosphorylated amino acids are separated and analyzed by capillary electrophoresis. Linear correlation coefficients of all three O-phosphorylated amino acids to their UV absorbance values were greater than 0.992 (n = 6) in the 25 to 250 pmol / μl concentration range. Method detection limit at the fmol level. Using this method, the phosphorylation sites of three model phosphopeptides and the native phosphoproteins β-casein and phosvitin were analyzed.