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本文采用（异）硫氰酸化学法，以乙酸酐为活化试剂，四丁铵硫氰酸为偶联试剂，溴甲基萘为烷化试剂，将蛋白质或多肽的Ｃ端依次转化并裂解为ＡＴＨ－氨基酸，在２５４ｎｍ进行检测。分析了若干种天然的、基因工程表达的蛋白质或多肽，测定了不同长度的Ｃ端序列，并确证了Ｃ端的修饰及突变情况。为蛋白质和多肽的完整性、均一性，基因工程产品及合成多肽的质控提供了重要的Ｃ端信息。目前，可在１～２ｎｍｏｌ水平上测定３～５个Ｃ端残基，个别蛋白质可测１０个以上残基。
In this paper, (different) thiocyanate chemical method, acetic anhydride as an activating reagent, tetrabutylammonium thiocyanate as a coupling reagent, bromomethyl naphthalene as an alkylating reagent, the C-terminal protein or polypeptide were sequentially converted and cleaved into ATH-amino acids at 254 nm. A number of native, genetically engineered proteins or polypeptides were analyzed, C-terminal sequences of different lengths were determined and confirmation of C-terminal modifications and mutations was made. Provides important C-terminal information for protein and polypeptide integrity, homogeneity, quality control of genetically engineered products and synthetic peptides. At present, 3 ~ 5 C-terminal residues can be measured at the level of 1 ~ 2 nmol, and more than 10 residues can be measured on individual proteins.