Two peptides (Im pr-M, Im ch-M) derived from Im ${lambda}-type$ of Bence Jones Protein and one peptide (Ikch-M) from Ik were separated and purified using the Dowex $50{ imes}2$ column $(1{ imes}20;cm)$ and Dowex $1{ imes}2(0.9{ imes}50;cm)$. The buffer solution was composed of 1% pyridine and IM formic acid in Dowex $1{ imes}2$ column. The blocked N-terminal was examined with ninhydrin reaction before and after alkaline hydrolysis, which was fractionated by Dowex $1{ imes}2$ column. Pyrro-glutamic acid in N-terminal residue was identified by comparing with the authentic pyrro-glutamic acid through a high voltage electrophoresis (pH 3.5, 3000 V.) after the peptide Im pr-M (PCA. Ser) was cleavaged at the position of serine with cone. (12 N) HCl and the pyrro-glutamic acid was converted to glutamic acid by treating it with N-NaOH for 116 hours at $27^{circ}C$. The substractive method was applied to find out the sequence of peptides and carboxypeptidase A was employed to release C-terminal residue from the peptide. In present study PCA. Ser in Im Pr-M was isolated from the pronase digested ${lambda}$-type Bence Jones protein. The yield of the Im Pr-M was 79.6 percent of its theoretical value, based on the molecular weight of Bence Jones Protein. Im ch-M (PCA. Ser Val. Leu) was isolated from the chymotrypsin digested ${lambda}$-type Bence Jones Protein. The yield of the Im ch-M was 72.2 percent. based on the molecular weight of Bence Jones Protein. Ik ch-M (PCA. Ser. Ala. Leu) was isolated from the chymotrypsin digested ${lambda}$-type Bence Jones Protein and its yield was 42% based on the molecular weight of Bence Jones Protein.