Abstract
The basic subunit of cartilage proteoglycan consists of multiple glycosaminoglycan chains covalently attached to a core protein. It is unclear as to whether there is a single core protein or multiple different core proteins, since previous studies using either chondroitinase or testicular hyaluronidase to enzymatically remove chondroitin sulfate side chains from the proteoglycan subunit have yielded conflicting results. In the present study, a chon-droitinase-produced core protein preparation isolated as a single peak on Sepharose gel chromatography was found to contain at least two immunologically distinct components. Hyaluronidase-produced core protein from the same proteoglycan subunit fraction was found to contain multiple components nearly all of which were smaller than the components in the chondroitinase digest. A possible explanation of these findings is that they resulted from pro-teolytic degradation of the core protein in the course of the enzymatic removal of its chondroitin sulfate. The presence of small amounts of protease contaminants in several commercial chondroitinase and hyaluronidase preparations was detected by an extremely sensitive radioassay. Until proteases can be rigorously excluded from enzyme preparations used to degrade the proteoglycan subunit, it will not be possible to determine whether it consists of a single or several different core proteins.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 147-155 |
| Number of pages | 9 |
| Journal | Connective Tissue Research |
| Volume | 5 |
| Issue number | 3 |
| DOIs | |
| State | Published - 1977 |
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ASJC Scopus subject areas
- Biochemistry
- Cell Biology
- Molecular Biology
- Orthopedics and Sports Medicine
- Rheumatology
- Immunology
- Nephrology
Cite this
A comparison of bovine nasal cartilage proteoglycan core protein produced by chondroitinase and hyaluronidase : The possible role of protease contaminants. / Keiser, Harold D.; Hatcher, Victor Bernard.
In: Connective Tissue Research, Vol. 5, No. 3, 1977, p. 147-155.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A comparison of bovine nasal cartilage proteoglycan core protein produced by chondroitinase and hyaluronidase
T2 - The possible role of protease contaminants
AU - Keiser, Harold D.
AU - Hatcher, Victor Bernard
PY - 1977
Y1 - 1977
N2 - The basic subunit of cartilage proteoglycan consists of multiple glycosaminoglycan chains covalently attached to a core protein. It is unclear as to whether there is a single core protein or multiple different core proteins, since previous studies using either chondroitinase or testicular hyaluronidase to enzymatically remove chondroitin sulfate side chains from the proteoglycan subunit have yielded conflicting results. In the present study, a chon-droitinase-produced core protein preparation isolated as a single peak on Sepharose gel chromatography was found to contain at least two immunologically distinct components. Hyaluronidase-produced core protein from the same proteoglycan subunit fraction was found to contain multiple components nearly all of which were smaller than the components in the chondroitinase digest. A possible explanation of these findings is that they resulted from pro-teolytic degradation of the core protein in the course of the enzymatic removal of its chondroitin sulfate. The presence of small amounts of protease contaminants in several commercial chondroitinase and hyaluronidase preparations was detected by an extremely sensitive radioassay. Until proteases can be rigorously excluded from enzyme preparations used to degrade the proteoglycan subunit, it will not be possible to determine whether it consists of a single or several different core proteins.
AB - The basic subunit of cartilage proteoglycan consists of multiple glycosaminoglycan chains covalently attached to a core protein. It is unclear as to whether there is a single core protein or multiple different core proteins, since previous studies using either chondroitinase or testicular hyaluronidase to enzymatically remove chondroitin sulfate side chains from the proteoglycan subunit have yielded conflicting results. In the present study, a chon-droitinase-produced core protein preparation isolated as a single peak on Sepharose gel chromatography was found to contain at least two immunologically distinct components. Hyaluronidase-produced core protein from the same proteoglycan subunit fraction was found to contain multiple components nearly all of which were smaller than the components in the chondroitinase digest. A possible explanation of these findings is that they resulted from pro-teolytic degradation of the core protein in the course of the enzymatic removal of its chondroitin sulfate. The presence of small amounts of protease contaminants in several commercial chondroitinase and hyaluronidase preparations was detected by an extremely sensitive radioassay. Until proteases can be rigorously excluded from enzyme preparations used to degrade the proteoglycan subunit, it will not be possible to determine whether it consists of a single or several different core proteins.
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UR - http://www.scopus.com/inward/citedby.url?scp=0017720405&partnerID=8YFLogxK
U2 - 10.3109/03008207709152265
DO - 10.3109/03008207709152265
M3 - Article
C2 - 144580
AN - SCOPUS:0017720405
VL - 5
SP - 147
EP - 155
JO - Connective Tissue Research
JF - Connective Tissue Research
SN - 0300-8207
IS - 3
ER -