| Abstract: | Treatment of highly purified preparations of the third component of complement (C3) with 0.5M hydroxylamine at 20 degrees C for 15 to 30 minutes, followed by acidification, resulted in dissociation of a peptide from the C3 molecule. The isolated fragment (molecular weight, 7600) resembled enzymatically liberated anaphylatoxin (C3a) with respect to size, charge, amino acid composition, and biological activity. Its capacity to contract smooth muscle was inhibitable by antihistamines; it also produced tachyphylaxis and desensitization of the guinea pig ileum to C3a. Thus native C3 probably contains an esterlike bond and hydroxylamine-liberated anaphylatoxin may represent one of the polypeptide chains of the C3 molecule. |
