Hyaluronidase dermatan sulfate

Dermatan sulfate (condroitin sulfate B from pig skin) [54328-33-5 (Na salt)]. Purified by digestion with papain and hyaluronidase, and fractionation using aqueous EtOH. [Gifonelli and Roden Biochem Prep 12 1 1968.]... 

Several studies have shown that hyaluronidase is iidiibited by ft1, Fe Cu +, Ag+, Hg2+, Zn2+, Cd2+, and Pb2+ salts [26,51,58,77,78]. Substrate analogs like chondroitin sulfate tit desulfeted chondroitin sulfate B, dermatan sulfate, keratan sulfate, heparitin sulfate, and heparin were shown to be competitive inhibitors of hyaluronidase [14,54]. 

Dermatan sulfate may be distinguished from chondroitin 4- and 6-sulfates in that it is not degraded by testicular hyaluronidase and, furthermore, the desulfated mucopolysaccharide is unattacked by testicular and bacterial hyaluronidases (M17). Further diflFerentiation of dermatan sulfate from hyaluronic acid and the foregoing chondroitin sulfates is readily made on the basis of color reactions given by the different uronic acid components. Dermatan sulfate shows equimolar ratios of uronic acid ihexosamine sulfate when the uronic acid content is determined by the orcinol (K7) or decarboxylation (T4) methods, whereas significantly lower values are obtained by the carbazole method (D8). 

Commercial preparations usually contain this type of hyaluronidase. The enzyme is found in testicular tissue of most mammals and is located in the acrosomal cap of spermatozoa [6], Testicular hyaluronidase degrades hyaluronan, chondroitin, chondroitin-4- and -6-sulfate to oligosaccharides, mainly tetrasaccharides [1]. Partial degradation of dermatan sulfate has been described [7]. Testicular hyaluronidase had a broad pH range of activity [5]. 

Bollet et al. [11] demonstrated the presence of hyaluronidase activity in various mammalian tissues. They showed that this type of hyaluronidase differed from the testicular type concerning pH optimum and pH range of activity. Subsequent studies revealed that the enzyme was present in the lysosomal fraction of the tissues [12]. The liver is an especially rich source [13]. Degradation of hyaluronan leads to the same end products as testicular hyaluronidase [11]. Lysosomal hyaluronidase from rat liver degrades chondroitin-4- and -6-sulfate, but not dermatan sulfate, desulfated dermatan sulfate, heparan sulfate, keratan sulfate, or heparin [14], Lysosomal hyaluronidase has an acid pH optimum and a narrow pH range of activity [14]. This difference in pH profile of activity has commonly been used to differentiate between testicular and lysosomal hyaluronidase. A similar acid-active hyaluronidase is present in human serum [15]. 

Hyaluronidase from bee venom has about the same substrate specificity as snake hyaluronidase [19]. Venom of social wasps was found to contain high levels of hyaluronidase activity, whereas venom from ants contains low levels of activity [20]. Lizard venom contains a hyaluronidase that acts almost specific on hyaluronan, i.e., it has no activity toward chondroitin-6-sulfate, dermatan sulfate, or heparin and only weak activity toward chondroitin-4-sulfate [21]. 

A hyaluronidase has been purified and characterized from stonefish (Synanceja horrida) venom. It acts specifically on hyaluronan, producing tetra-, hexa-, octa-, and decasaccharides, but does not act on chondroitin sulfate or dermatan sulfate [22,23]. 

Hyaluronidase from Flavobacterium and Proteus vulgaris has been shown to hydrolyze chondroitin-4- and -6-sulfate and to possess weak activity toward dermatan sulfate [30], Hyaluronidase from Streptomyces hyalumlyticus... 

The presence of a-hexosaminide bonds presumably accounts for the inactivity of hyaluronidases toward hepmin (L) and heparan sulfate, whereas the lack of an appropriately orientated uronic acid residue may prevent the action of hyaluronidase upon kcratan sulfate (XXXXIX), the principal repeating unit of dermatan sulfate (XXXXVII), and teich-uronic acid (janezura ei al., 1961), (an a ucuronosyl-iV -acetyl- alactos-amine polymer) (Hughes, 1970 Hughes and Thunnan, 1970). 

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