Yanaihara C, Matsumoto T, Hong Y M, Yanaihara N
FEBS Lett. 1985 Sep 9;189(1):50-6. doi: 10.1016/0014-5793(85)80840-1.
Using a radioimmunoassay specific for porcine glicentin C-terminal hexapeptide, we isolated a peptide from porcine pancreas and characterized it as the C-terminal 64-69 sequence of glicentin: H-Asn-Lys-Asn-Asn-Ile-Ala-OH. The purification steps included gel filtration, ion-exchange chromatography and HPLC. In each step, the recovery of the desired peptide, radioimmunologically estimated from the respective elution profile, was 71.4-91.7%. The final yield of the hexapeptide was 22 micrograms (4.3%) from 800 g pancreas. The pancreatic content of this peptide was estimated to be approximately equimolar to that of pancreatic glucagon. No hexapeptide-like component was detected in porcine intestinal extracts. The data confirmed that the processing of pancreatic proglucagon liberates the C-terminal hexapeptide of the intramolecular glicentin sequence in a tissue-specific manner during the production of glucagon.
使用针对猪胰高血糖素C端六肽的放射免疫分析法，我们从猪胰腺中分离出一种肽，并将其鉴定为胰高血糖素的C端64 - 69序列：H-Asn-Lys-Asn-Asn-Ile-Ala-OH。纯化步骤包括凝胶过滤、离子交换色谱和高效液相色谱。在每个步骤中，根据各自的洗脱曲线通过放射免疫法估算的所需肽的回收率为71.4 - 91.7%。从800克胰腺中得到的六肽最终产量为22微克（4.3%）。该肽在胰腺中的含量估计与胰高血糖素的含量大致等摩尔。在猪肠道提取物中未检测到类似六肽的成分。数据证实，在胰高血糖素产生过程中，胰腺前胰高血糖素的加工以组织特异性方式释放分子内胰高血糖素序列的C端六肽。
