Hyaluronidase properties

Echinacea extracts appear to stimulate the number and activity of immune cells (i.e., increasing physiological levels of tumor necrosis factor and other cytokines) and to increase leukocyte mobility and phagocytosis. The extracts also have antiviral and antiinflammatory properties and inhibit bacterial hyaluronidase. 

Certain echinacea constituents have demonstrated anti-inflammatory properties in vitro. Inhibition of cyclooxygenase, 5-lipoxygenase, and hyaluronidase may be involved. In animals, application of Epurpurea prior to application of a topical irritant reduced both paw and ear edema. Despite these laboratory findings, randomized, controlled clinical trials involving echinacea for wound healing have not been performed in humans. 

Lysosomal hyaluronidase possesses transglycosylation properties using octo-saccharides as a substrate, rather than hexasaccharides like testicular hyaluronidase [14, lti]. 

In this chapter we describe some methods used to determine the kinetics of the action of hyaluronidase. Thble 2 presents a survey of the Michaelis-Menten constants (Km) of the action of hyaluronidase on hyaluronan and chondiootin sulfate obtained using different methods. These assays usually make use of hyaluronan as a substrate for hyaluionidase. Various sources of hyalmonan are employed, but these arbitrates have different physicochemical properties (molecular weight intrinsic viscosity). Payan el al [130] investigated the action of Streptmnyces hyahnonidase on hyaluronan from several sources. 

G. S. Gupta and E. Goldberg. Isolation, properties, immunological specificity and localization of mouse testicular hyaluronidase. Blochim. Blaphys. Acta 57 364 (1981). 

C. perfringens is the most important of the histotoxic clostridia that cause tissue infections in humans, especially of the muscle tissue (clostridial myonecrosis or gas gangrene). The organism is more aerotolerant than most other anerobes. In addition to toxins and enzymes, many of which have lethal, cell-destroying and hemolytic properties, a number of nonlethal enzymes are also produced and apparently contribute to the invasiveness of the organism in the tissue. These include collagenase, deoxyribonuclease, and hyaluronidase. 

Animal venoms usually possess hyaluronidase activity [17]. The enzymatic properties, including hyaluronidase, of snake venoms have been extensively studied by Tan et al. [18]. Snake hyaluronidase acts on hyaluronan, chondroitin, and chondroitin-4- and -6-sulfate, producing various oligosaccharides, mainly tetrasaccharides [1]. 

Table 1 presents a survey of hyaluronidase activity in the venom of several animal species. Transglycosylation properties have been observed with hyaluronidase from snake venom (Crotalus terrificus) [8], but not with hyaluronidase from bee venom [19]. 

Hyaluronidase has an absolute requirement for cations, as dialyzed preparations show no activity toward dialyzed substrates. K+, Na+, Ca2+, Mg2+, and Mn2+ all have stimulating properties toward hyaluronidase. The monovalent cations show the strongest stimulating effects and act over a broader range of concentration than divalent cations [50]. Testicular, serum, and lysosomal hyaluronidase seem to have different sensitivities toward NaCl [54,61]. A noncompetitive mechanism was proposed to explain the activation of hyaluronidase by Na+ [59,62]. 

Figure 3 Inhibition properties of some flavonoids (250 mM) on hyaluronidase from several venom sources and from bovine testes. (From Refs. 80,81.)...

M. Budds, J. Edwards, A. H. Olavesen, and P. Gacesa. A comparison of the properties of the hyaluronidases from a temperate and a tropical species of leech. Comp. Biochem. Physiol. 576 497 (1987). 

C. Yang and P. N. Srivastava. Purification and properties of hyaluronidase from bull sperm. J. Biol. Chem. 250 19 (1975). 

L. J. D. Zaneveld, K. L. Polakoski, and G. F. B. Schumacher. Properties of acrosomal hyaluronidase from bull spermatozoa evidence for its similarity to testicular hyaluronidase. J. Biol. Chem. 248 564 (1973). 

E. W. Gold. Purification and properties of hyaluronidase from human liver. Biochem. J. 205 69 (1982). 

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