Flengsrud R
Int J Pept Protein Res. 1979 May;13(5):498-509. doi: 10.1111/j.1399-3011.1979.tb01912.x.
A method for quantitation of amino-terminal residues in proteins is presented. The method is a modification of a double isotope-labelling technique, using 3H-labelled dansyl chloride and 14C-labelled amino acids as internal standards. The method is demonstrated on human fibrinogen, horse myoglobin and on mouse myoloma IgA. A linear relationship between the ratio 3H/14C in the separated amino-terminal amino acid of the protein and the amount of protein added in the labelling mixture was obtained with standard deviations of +/- 7.4% +/- 3.4% and +/- 10.3%, respectively. An application of the method is demonstrated by measuring the increase in amino-terminal glycine in fibrinogen following the proteolytic action of thrombin. The method seems to be useful when 0.1 nmol or more of protein is used.
本文介绍了一种蛋白质氨基末端残基的定量方法。该方法是对双同位素标记技术的改进，使用³H标记的丹磺酰氯和¹⁴C标记的氨基酸作为内标。该方法已在人纤维蛋白原、马肌红蛋白和小鼠骨髓瘤IgA上得到验证。在标记混合物中加入的蛋白质与分离得到的蛋白质氨基末端氨基酸中³H/¹⁴C的比值之间呈线性关系，其标准偏差分别为±7.4%、±3.4%和±10.3%。通过测量凝血酶蛋白水解作用后纤维蛋白原中氨基末端甘氨酸的增加，证明了该方法的应用。当使用0.1 nmol或更多的蛋白质时，该方法似乎很有用。
