Abstract
Summary
The antibacterial and antiviral properties of a tissue polypeptide were compared with the activity of a synthetic lysine polypeptide. On a weight basis, the activity of the synthetic peptide was approximately 4 times greater than that of the natural peptide. From the fact that the tissue peptide contains 30% lysine, it is possible to conclude that the activity resides within the lysine portion of the molecule. Additional evidence to support the implication of lysine was obtained from a comparative study on the mode of inactivation of these peptides by desoxy-ribonucleic acid (DRNA) and ribonucleic acid (RNA). Both peptides combine stoich-iometrically, at pH 6.5 with DRNA but not with RNA; it is apparent that both peptides combine with RNA in multiple proportions depending upon the relative concentrations of the reactants. In this respect, the similarity between the RNA-peptide interaction and antigen-antibody reactions is pointed out. A mechanism by which the tissue polypeptide could take part in the natural resistance of animals to infection and the possible role of these basic peptides in fibrinoid degeneration is discussed.
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