Abstract
By purifying the dried powder, which was precipitated from the human saliva by the addition of acetone, as shown in Fig. 1, parotin-like protein was isolated and named “Saliva-parotin”.
Its isoelectric point was pH 3.4 and its purity in the electrophoretic analysis was 72.7%(by the ascending).
It gave all the color reactions of proteins and precipitated with acids or heavy metals, but did not coagulate in aqueous solution by heating.
By paper partition chromatogrophy of the hydrolyzate of saliva-parotin seventeen kinds of amino acids were identified. Saliva-parotin possesses an entirely the same biological action as parotin; decrease of serum calcium level, promotion of calcifying the incisor dentine, increase of the number of circulating leueocytes and rise of the bone marrow temperature were clearly observed in rabbits. The fall of the blood pressure in an anesthetized dog was recognized with an insufficiently purified preparation, but not in the case of the preparation with 72.7% purity.
Acknowledgement. The authors greatly appreciative of the cooperation of Dr. H. Takatani, Tasaka Internal Medical Department, University of Tokyo, Prof. S. Huse and Mr. N. Matsuda, Department of Dental Surgery, School of Medicine, Gunma University, Mr. H. Takigawa, Endocrinological Laboratory, School of Medicine, Gunma University, and Mr. Y. Morioka, Teikoku Hormone Manufacturing Co., and co-workers in this study.
