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J Dent Res 49(3): 561-566, 1970
© 1970 International and American Associations for Dental Research
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Purification and Properties of Acid Phosphomonoesterase from Human Parotid Saliva

RYO NAKAMURA 1, TATSUO WATANABE 1, YOSHIFUMI IW AMOTO 1, and AKIRA TSUNEMITSU 1

1 Department of Preventive Dentistry, Hiroshima University School of Dentistry, Hiroshima, Japan

Acid phosphomonoesterase was separated from human parotid saliva and purified. The purified enzyme was proved homogeneous on sedimentation and disk electrophoresis. The optimal pH of the enzyme was 3.3. The enzyme had no substrate specificity for phosphomonoesters and its activity was inhibited by SnF2 or NaF.

Submitted on May 27, 1969






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