Abstract
Hyaluronidases are a group of enzymes that degrade the glycosaminoglycan hyaluronan (HA, hyaluronic acid). Many types of hyaluronidases are reported, from prokaryotes to eukaryotes (1,2). These enzymes have a wide variety of properties, including substrate specificity, inhibitor sensitivity, and a range of pH optima. Streptomyces hyaluronidase, and the venom hyaluronidases from bee, snake, and scorpion are active at neutral pH. Hyal-1, the best-characterized somatic hyaluronidase (3–5), product of one of the six hyaluronidase-like sequences in the human genome (6), is an acid-active enzyme with an optimum at pH 3.7. The sperm-specific PH-20 (7) has apparently two pH optima, pH 4.5 and 7.5, resulting possibly from two forms of the enzyme, membrane-bound and soluble (8,9)
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Mio, K., Csóka, A.B., Stair, S.N., Stern, R. (2001). Detecting Hyaluronidase and Hyaluronidase Inhibitors. In: Iozzo, R.V. (eds) Proteoglycan Protocols. Methods in Molecular Biology™, vol 171. Humana Press. https://doi.org/10.1385/1-59259-209-0:391
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DOI: https://doi.org/10.1385/1-59259-209-0:391
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