heptapeptide upon HCL hydrolysis produced equimolar amounts of ASP, CYS, GLU, LYS, PHE, TYR, VAL and ammonia. Exposure of the intact heptapeptide to FDNB followed by hydrolysis produced DNP-VAL. Treatment with trypsin produced a tripeptide , T1 and a tetrapeptide, T2. T2 had an absorbance peak near 260 nm and produced ammonia on hydrolysis. T1 had an absorbance peak near 275 nm ( which was greater than that of T1) and tested positive for sulfur. Exposure of the heptapeptide to chymotrypsin produced two tripeptides ( CT1 and CT2) which both had UV absorbances and ASP. CT1 contained sulfur and had the greater absorbance of the two chymotrypsin produced tripeptides. CT2 produced ammonia upon hydrolysis. When exposed to electrophoresis at pH6, T2, and CT1 were cations, T1 was an anion, and CT2 has essentially no charge. Deduce the sequence of the heptapeptides from the data.