Rouimi P, de Caro J, Bonicel J, Rovery M, de Caro A
Centre de Biochimie et de Biologie Moléculaire, CNRS, Marseille, France.
FEBS Lett. 1988 Feb 29;229(1):171-4. doi: 10.1016/0014-5793(88)80820-2.
Following the complete sequence elucidation of human pancreatic stone protein (immunoreactive form PSP S1 isolated from pancreatic juice) [(1987) Eur. J. Biochem. 168, 201-207], the location of the three S-S bridges of the protein was investigated. The cystine-containing peptides, detected after the separation of the peptic or chymotryptic digests on SP-Sephadex or Sephadex G-50, were submitted to Edman degradation and/or to oxidation. The cysteic peptides after separation on SP-Sephadex or Sephadex G-50 were characterized by their amino acid compositions. The pairing of the half-cystines: Cys 3-Cys 14, Cys 31-Cys 129 and Cys 104-Cys 121 was determined. The same experiments carried out with PSP S2-5 (other immunoreactive forms) gave an identical characterization.
在完成人胰石蛋白（从胰液中分离出的免疫反应形式PSP S1）的完整序列解析[(1987)《欧洲生物化学杂志》168, 201 - 207]之后，对该蛋白的三个二硫键位置进行了研究。在SP - Sephadex或Sephadex G - 50上分离胃蛋白酶或胰凝乳蛋白酶消化产物后检测到的含胱氨酸肽段，进行了埃德曼降解和/或氧化处理。在SP - Sephadex或Sephadex G - 50上分离后的半胱氨酸磺酸肽段通过其氨基酸组成进行表征。确定了半胱氨酸的配对情况：Cys 3 - Cys 14、Cys 31 - Cys 129和Cys 104 - Cys 121。用PSP S2 - 5（其他免疫反应形式）进行的相同实验给出了相同的表征结果。
