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Identification of Hyaluronidase Activity in Rabbit Dental Pulp
N. Sakamoto
Department of Endodontology and Periodontology
T. Nakajima
Department of Endodontology and Periodontology
K. Ikunaga
Department of Endodontology and Periodontology
H. Shidahara
Department of Endodontology and Periodontology
H. Okamoto
Department of Endodontology and Periodontology
K. Okuda
Department of Biochemistry, Hiroshima University School of Dentistry, 1-2-3 Kasumi, Minami-ku, Hiroshima 734, Japan
A hyaluronidase activity was demonstrated in rabbit dental pulp. The optimum pH of the enzyme was 3.8. The enzyme activity was enhanced by protamine and poly-L-lysine and was inhibited by iodoacetamide, ferric ion, and ferrous ion in decreasing order. The product of the enzyme reaction was identified as tetrasaccharide. From these results it was concluded that the enzyme exists in pulp tissue and is functioning for degradation of proteoglycans in situ.
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Journal of Dental Research, Vol. 60, No. 4,
850-854 (1981)
DOI: 10.1177/00220345810600041601

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C.N. Bertolami and D.G. Ellis
Identification and Characterization of Rabbit Buccal Mucosal Hyaluronidase
Journal of Dental Research,
June 1, 1985;
64(6):
913 - 918.
[Abstract]
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