412
PETER BERNFELD
other polysaccharide hydrolyzing enzymes, but it is not infrequent in
other hydrolytic enzymes.
Hyaluronidase is further distinct from the other polysaccharidases
by its physiological action on the capillary permeability, a reaction
unique not only among hydrolases.
C. HEPARINASE
A soil bacterium identified as Flavobacterium has been isolated in
pure form, which is able to use heparin as its sole source of carbon,
nitrogen, and sulfur (339). It is implied that this microorganism must
contain an enzyme capable of depolymerizing heparin, although the
mechanism of this reaction is still unknown. The presence of heparinase
in tissue extracts, in particular from rabbit liver, has been reported by
Jaques (340). This author measured heparinase activity by the disappearance of the anticoagulant activity of the substrate. The nature of
the chemical reaction underlying this inactivation is still unknown; it
does not necessarily have to be a depolymerization reaction, although
this appears to be quite likely.
D. CHONDROITINASE
Two enzymes appear to be involved in the breakdown of chondroitin
sulfate from cartilage. A successful separation of these two enzymes
has been achieved by Dodgson and Lloyd (341). They observed that
the hydrolysis of sulfate ester groups by chondrosulfatase is not a prerequisite for the depolymerization of the substrate by chondroitinase,
but the activity of the sulfatase is greatly enhanced by preliminary
degradation of the polysaccharide chain. This indicates that the depolymerization must be the primary reaction whereby the formation of
sulfated oligosaccharides can be anticipated.
Chondroitinase has been found in Proteus vulgaris (341), and the
presence of this enzyme in association with the sulfatase was also
reported in other bacteria (342) and in mollusks (343).
The degradation of chondroitin sulfate by certain hyaluronidase
preparations has been reported in the literature (344). It is not known,
however, whether these enzyme sources contain a specific chondroitinase in addition to hyaluronidase, or whether the specificity of hyaluronidase in these preparations has a broad spectrum of substrate
specificity which would also include chondroitin sulfate.
E. LYSOZYME
Lysozyme is the example of an enzyme which was discovered (64)
through its physiological action (dissolution of certain bacterial cells),
PETER BERNFELD
other polysaccharide hydrolyzing enzymes, but it is not infrequent in
other hydrolytic enzymes.
Hyaluronidase is further distinct from the other polysaccharidases
by its physiological action on the capillary permeability, a reaction
unique not only among hydrolases.
C. HEPARINASE
A soil bacterium identified as Flavobacterium has been isolated in
pure form, which is able to use heparin as its sole source of carbon,
nitrogen, and sulfur (339). It is implied that this microorganism must
contain an enzyme capable of depolymerizing heparin, although the
mechanism of this reaction is still unknown. The presence of heparinase
in tissue extracts, in particular from rabbit liver, has been reported by
Jaques (340). This author measured heparinase activity by the disappearance of the anticoagulant activity of the substrate. The nature of
the chemical reaction underlying this inactivation is still unknown; it
does not necessarily have to be a depolymerization reaction, although
this appears to be quite likely.
D. CHONDROITINASE
Two enzymes appear to be involved in the breakdown of chondroitin
sulfate from cartilage. A successful separation of these two enzymes
has been achieved by Dodgson and Lloyd (341). They observed that
the hydrolysis of sulfate ester groups by chondrosulfatase is not a prerequisite for the depolymerization of the substrate by chondroitinase,
but the activity of the sulfatase is greatly enhanced by preliminary
degradation of the polysaccharide chain. This indicates that the depolymerization must be the primary reaction whereby the formation of
sulfated oligosaccharides can be anticipated.
Chondroitinase has been found in Proteus vulgaris (341), and the
presence of this enzyme in association with the sulfatase was also
reported in other bacteria (342) and in mollusks (343).
The degradation of chondroitin sulfate by certain hyaluronidase
preparations has been reported in the literature (344). It is not known,
however, whether these enzyme sources contain a specific chondroitinase in addition to hyaluronidase, or whether the specificity of hyaluronidase in these preparations has a broad spectrum of substrate
specificity which would also include chondroitin sulfate.
E. LYSOZYME
Lysozyme is the example of an enzyme which was discovered (64)
through its physiological action (dissolution of certain bacterial cells),