| Abstrakt: |
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) [ABSTRACT FROM AUTHOR] |
