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Using rather simple and mild extraction and separation methods, three ovine pineal fractions (XM 300 R-PP7.2' and PP7.2 S) were obtained, which contain peptidic/proteic substances and which show fluorescence characteristics of indoles. The ovine fractions were compared with the bovine pineal E-5 fraction. The ovine fractions are chemically sensitive to normal laboratory light and stable in red light (lambda greater than 600 nm). Immunologically, these fractions and the bovine E 5 fraction are stable. From the results of radioimmunological experiments it was concluded that the bovine pineal E 5 fraction as well as the ovine pineal fraction XM 300 R-PP7.2 and PP7.2S may contain (a) peptide(s) ending by the same carboxy terminal tripeptide Pro-Arg-Gly(NH2).

The vasotocin-like biological activity detected in an extract (E5 fraction) of bovine pineal gland was found not to be due to the presence of vasotocin, vasopressin or oxytocin. The data obtained by means of bio- and radioimmunoassays suggest that the peptide responsible for this biological activity, however, possess the same Pro-Arg-Gly(NH2) tripeptidic carboxy-terminal end as vasotocin.