Studies on sequencing of peptides from the carboxyl terminus by using the thiocyanate method

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Abstract
We report on our experience in applying the thiocyanate method developed by Stark (1968) (Biochemistry 7, 1796-1807) to the sequencing of short peptides from the carboxyl end in free solution. Yields fell to very low levels after three cycles of degradation. The method was time-consuming because of the filtration and freeze-drying stages involved. To overcome these problems, peptides were attached to modified polystyrene polymers for sequential degradation in the solid phase, and a maximum of six amino acids was determined. Also, ribonuclease was attached to active-ester glass beads and sequential degradation was carried out to determine six amino acids at the C-terminal end of this protein.