Arzamazova N M, Aristarkhova E A, Shafieva G I, Nazimov I V, Aldanova N A
Bioorg Khim. 1985 Dec;11(12):1598-606.
The selective tryptic digestion of the native membrane-bound enzyme was carried out under conditions that provide the extensive hydrolysis of hydrophilic regions of the alpha-subunit into small fragments and allow to preserve the integrity of the beta-subunit. Twenty-seven water-soluble peptides comprising approximately 40% of the total polypeptide chain were isolated by HPLC and their complete or partial amino acid sequence was determined. It led to general outline of the structural organisation of the alpha-subunit hydrophilic regions exposed from membrane. The information thus obtained was used in synthesis of specific oligonucleotide probes.
在能使α亚基的亲水区域广泛水解成小片段并保持β亚基完整性的条件下，对天然膜结合酶进行了选择性胰蛋白酶消化。通过高效液相色谱法分离出了27种水溶性肽，它们约占总多肽链的40%，并测定了其全部或部分氨基酸序列。这得出了从膜中暴露的α亚基亲水区域的结构组织概况。由此获得的信息被用于合成特异性寡核苷酸探针。
