TY - JOUR
T1 - Chondroitin sulfate-degrading enzymes in human polymorphonuclear leukocytes
T2 - Characteristics and evidence for concerted mechanism
AU - Buermann, Christine W.
AU - Oronsky, Arnold L.
AU - Horowitz, Martin I.
N1 - Funding Information:
Support from NIH research Grant AM 15475-08 to Dr. M. Horowitz from the National Institute of Arthritis, Metabolism and Digestive Diseases is gratefully acknowledged. The authors also wish to thank Ms. Vanda Garti her assistance in preparing this manuscript.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1979/3
Y1 - 1979/3
N2 - Human polymorphonuclear leukocyte-derived enzymes, β-glucuronidase, β-N-acetylgalactosaminidase, and aryl sulfatase were studied for their ability to degrade chondroitin sulfate. Evidence is presented which implies a concerted, synergistic mechanism of action for these enzymes in glycosaminoglycan degradation excluding the possibility of endoglycosidase activity. Conclusions are based upon results derived from pH optimum, inhibitor studies, kinetics, and partial purification of these enzymes. The data presented here demonstrate that the polymorphonuclear leukocytes contain all of the enzymes necessary for the solubilization and complete degradation of the chondroitin-4-sulfate of cartilage matrix.
AB - Human polymorphonuclear leukocyte-derived enzymes, β-glucuronidase, β-N-acetylgalactosaminidase, and aryl sulfatase were studied for their ability to degrade chondroitin sulfate. Evidence is presented which implies a concerted, synergistic mechanism of action for these enzymes in glycosaminoglycan degradation excluding the possibility of endoglycosidase activity. Conclusions are based upon results derived from pH optimum, inhibitor studies, kinetics, and partial purification of these enzymes. The data presented here demonstrate that the polymorphonuclear leukocytes contain all of the enzymes necessary for the solubilization and complete degradation of the chondroitin-4-sulfate of cartilage matrix.
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U2 - 10.1016/0003-9861(79)90032-8
DO - 10.1016/0003-9861(79)90032-8
M3 - Article
AN - SCOPUS:0018428364
SN - 0003-9861
VL - 193
SP - 277
EP - 283
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -