TY - JOUR
T1 - A heparan sulfate-degrading endoglycosidase from rat liver tissue
AU - Höök, Magnus
AU - Wasteson, Åke
AU - Oldberg, Åke
N1 - Funding Information:
This investigation was supported by qrants frcxn the Swedish Medical Research Council (13X 2309, 13X 44861, The Swedish Cancer Society (53) and Gustav V:s 80-brstind.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1975/12/15
Y1 - 1975/12/15
N2 - Incubation of a rat liver lysosomal fraction with [35S]heparan sulfate resulted in degradation of the polymer to oligosaccharides, demonstrating the presence of a heparan sulfate-degrading endoglycosidase. Judging from the size of the oligosaccharides, representing degradation end-products, only a limited number of the glycosidic linkages in the heparan sulfate molecule would seem to be susceptible to the heparitinase. The pH-dependence of the enzyme (active at pH 5.6; inactive at pH 3.8) was found to differ from that of liver hyaluronidase (active at pH 3.8; inactive at pH 5.6), suggesting that the heparitinase is a previously unknown enzyme.
AB - Incubation of a rat liver lysosomal fraction with [35S]heparan sulfate resulted in degradation of the polymer to oligosaccharides, demonstrating the presence of a heparan sulfate-degrading endoglycosidase. Judging from the size of the oligosaccharides, representing degradation end-products, only a limited number of the glycosidic linkages in the heparan sulfate molecule would seem to be susceptible to the heparitinase. The pH-dependence of the enzyme (active at pH 5.6; inactive at pH 3.8) was found to differ from that of liver hyaluronidase (active at pH 3.8; inactive at pH 5.6), suggesting that the heparitinase is a previously unknown enzyme.
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U2 - 10.1016/0006-291X(75)90185-0
DO - 10.1016/0006-291X(75)90185-0
M3 - Article
C2 - 1035
AN - SCOPUS:0016816915
SN - 0006-291X
VL - 67
SP - 1422
EP - 1428
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -