Abstract
1. The fraction CS-5, extracted and isolated from bovine Harderian gland as the protein component increasing the serum alkaline phosphatase activity of rabbit was further purified by column chromatography using DEAE-cellulose. Resultant fraction CS-5d had almost activity that increases the serum alkaline phosphatase activity contained initially in CS-5, and was affirmed to be almost homogeneous protein through ultracentrifugal and electrophoretic analyses. 2. The sedimentation constant of CS-5d was 2.26×10-13. 3. The isoelectric point of CS-5d was found to be between pH 4.7 and 4.8. 4. The molecular weight of CS-5d was estimated as be 27, 000 by the Archibald's method.
