Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1995-7-20
|
pubmed:abstractText |
UDP-D-Galactose:D-xylose galactosyltransferase (Galactosyltransferase-I) is an enzyme involved in the synthesis of the linkage region of chondroitin sulfate. Measurement of galactosyltransferase-I in mature articular cartilage has depended on milling such tissue in liquid nitrogen to break open the cells and enable interaction of exogenous substrates with galactosyltransferase-I. This process requires large amounts (approximately 1 g wet wt) of cartilage. This paper reports the development of an assay for galactosyltransferase-I in articular cartilage where 10-25 mg (wet wt) of the tissue was extracted with a buffer containing the detergent Thesit. This assay was more time efficient, required less tissue, and was linear for up to 6 h. It was effective on both mature bovine articular cartilage and embryonic chick epiphyseal cartilage, detecting 100 and 68% of total galactosyltransferase-I activity, respectively. The higher number of measurements available allowed kinetic studies to be conducted on bovine articular cartilage explant cultures under conditions of up- and down-regulation. Incubation with fetal calf serum resulted in an increase in galactosyltransferase-I activity. Galactosyltransferase-I activity, however, did not change markedly in cartilage cultured in the absence of fetal calf serum or in the presence of cycloheximide. A soluble preparation of galactosyltransferase-I, extracted from bovine articular cartilage using Thesit, eluted from a Superose-6 column, with a molecular mass of about 55 kDa.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Cycloheximide,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Polyethylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/polidocanol,
http://linkedlifedata.com/resource/pubmed/chemical/xylosylprotein...
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0003-2697
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
20
|
pubmed:volume |
226
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
154-60
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:7785767-Animals,
pubmed-meshheading:7785767-Cartilage, Articular,
pubmed-meshheading:7785767-Cattle,
pubmed-meshheading:7785767-Chick Embryo,
pubmed-meshheading:7785767-Culture Media,
pubmed-meshheading:7785767-Culture Techniques,
pubmed-meshheading:7785767-Cycloheximide,
pubmed-meshheading:7785767-Detergents,
pubmed-meshheading:7785767-Enzyme Stability,
pubmed-meshheading:7785767-Galactosyltransferases,
pubmed-meshheading:7785767-Kinetics,
pubmed-meshheading:7785767-Polyethylene Glycols
|
pubmed:year |
1995
|
pubmed:articleTitle |
An assay for galactosyltransferase-I activity in articular cartilage.
|
pubmed:affiliation |
Department of Biochemistry, Monash University, Clayton, Victoria, Australia.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|