| Abstract: | The REMA method was found to be very suitable for the synthesis of secretin. The procedure was rapid, since on a 0.2 mmol-scale the rate of one amino acid per day could be attained, and yielded an unambiguous product after simple ion-exchange chromatography. REMA-secretin was found to be chemically identical with secretin prepared by fragment condensations and showed a biological activity of 3.4 (2.9–4.3) clinical units/μg, comparable to that of the natural product (4 clinical units/μg). The yield of purified secretin, a heptacosapeptide amide, calculated on the basis of C-terminal residue, amounted to 5%. |
