Abstract
A method for purifying from human tumor ascites fluid a dialysable polypeptide demonstrated to possess cell growth inhibiting effects is described. The process involves crystallization as a mercury complex. The purified polypeptide behaves during gel filtration as a substance with a mol. wt. of 1900–2000. The polypeptide is built up of 8 different amino acids and has glycine as N-terminal and leucine as C-terminal. It migrates in electrophoresis as one positively charged ninhydrin-positive band and behaves as one component during ion-exchange chromatography. By separation of the sub-peptides obtained by chymotryptic digestion 2 fractions were found. Tryptic digestion produced 3 separable fractions. The qualitative amino acid composition of the sub-peptides is given. The occurrence of two polypeptide fractions during some gel filtration procedures and its possible interpretation is described.
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