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Journal of Dental Research, Vol 60, 850-854, Copyright © 1981 by International & American Associations for Dental Research Online Journals
ARTICLES |
N. Sakamoto, T. Nakajima, K. Ikunaga, H. Shidahara, H. Okamoto and K. Okuda
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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