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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1987-3-4
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pubmed:abstractText |
Sialidase activity was assayed in homogenized rabbit alveolar macrophages using a fluorogenic substrate: sodium 4-methylumbelliferyl-alpha-D-neuraminate. After differential centrifugation one acid-active enzyme (optimum pH 4.2) was detected in the 16,000 X g pellet that contained lysosomes, mitochondria and peroxisomes. A second activity, with an optimum pH of 5.4, was found in the cytosolic fraction. The acid-active sialidase accounted for more than 95% of the total sialidase activity in crude homogenate. When alveolar macrophages were collected from rabbits stimulated with bacillus Calmette-Guerin (BCG), the acid-active sialidase specific activity was increased 2.5-fold whereas other lysosomal enzymes such as N-acetylglucosaminidase and beta-galactosidase were stable. The cytosolic sialidase activity did not change.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
923
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
150-5
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:3542051-Animals,
pubmed-meshheading:3542051-Cell Adhesion,
pubmed-meshheading:3542051-Cell Fractionation,
pubmed-meshheading:3542051-Cytosol,
pubmed-meshheading:3542051-Hydrogen-Ion Concentration,
pubmed-meshheading:3542051-Kinetics,
pubmed-meshheading:3542051-Lysosomes,
pubmed-meshheading:3542051-Macrophage Activation,
pubmed-meshheading:3542051-Macrophages,
pubmed-meshheading:3542051-Male,
pubmed-meshheading:3542051-Mycobacterium bovis,
pubmed-meshheading:3542051-Neuraminidase,
pubmed-meshheading:3542051-Pulmonary Alveoli,
pubmed-meshheading:3542051-Rabbits
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pubmed:year |
1987
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pubmed:articleTitle |
Lysosomal and cytosolic sialidases in rabbit alveolar macrophages: demonstration of increased lysosomal activity after in vivo activation with bacillus Calmette-Guerin.
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pubmed:publicationType |
Journal Article
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