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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1989-9-21
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pubmed:abstractText |
1. Two forms (I and II) with acidic pH optima and a neutral form of beta-hexosaminidase has been separated by DEAE-cellulose chromatography and characterized in skin and lung of 7, 9, 11, 14 day chick embryos and 1 day old chicken. 2. Forms I and II are similar to hexosaminidase A and B for their behaviour on DEAE-cellulose chromatography, Concanavalin A-Sepharose column and thermal stability. 3. Neutral form has a neutral pH optimum and higher molecular weight and a more acidic I. P. than forms I and II, a low beta-N-acetylgalactosaminidase activity and it is not bound by a Concanavalin A-Sepharose column and in that resemble hexosaminidase C and/or other neutral hexosaminidases. 4. We have found differences in the percentage of neutral form and in the specific activities of the extracts in the skin in different stages of development. 5. No significant differences were observed in the lung.
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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:issn |
0020-711X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
769-76
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:2527173-Animals,
pubmed-meshheading:2527173-Chick Embryo,
pubmed-meshheading:2527173-Chromatography, Liquid,
pubmed-meshheading:2527173-Enzyme Stability,
pubmed-meshheading:2527173-Hexosaminidase A,
pubmed-meshheading:2527173-Isoelectric Focusing,
pubmed-meshheading:2527173-Isoenzymes,
pubmed-meshheading:2527173-Lung,
pubmed-meshheading:2527173-Molecular Weight,
pubmed-meshheading:2527173-Morphogenesis,
pubmed-meshheading:2527173-Skin,
pubmed-meshheading:2527173-beta-N-Acetylhexosaminidases
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pubmed:year |
1989
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pubmed:articleTitle |
beta-N-acetylhexosaminidase isoenzymes during chick embryo development.
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pubmed:affiliation |
Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Università di Perugia, Italia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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