Michaelis-Menten constant hyaluronidase

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. 

Table 2 Michaelis-Menten (Km) Constants of the Action of Hyaluronidase from Different Sources on Different Substrates...

Type 3. Microbial hyaluronidases (e.g. Streptococcus hyaluronidase). Microbial hyaluronidases hydrolyse p-N-acetylaminoglycoside bonds of a substrate and simultaneously dehydrate the residue of uronic acid at the non-reducing terminus of the molecule. Substrate specificity of bacterial hyaluronate lyases varies considerably in the different species of microbe producers. Hyaluronidase of Streptococcus pneumoniae has the highest substrate specificity it hydrolyses HA alone and does not destroy other glucosami-noglycans [43]. The hyaluronate lyase, when isolated from Streptococcus pneumoniae, reaches optimal activity at pH 6.0 with the Michaelis constant with respect to HA being equal to 3.8x 10" mol/l (in terms of Michaelis-Menten kinetics) [44]. The presence of Cd3 (about 10 mM) is necessary in order to show the maximum enzyme activity. 

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See also in sourсe #XX -- [ ]

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