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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1989-6-8
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pubmed:abstractText |
The naturally occurring A2 activator protein for enzymic sphingolipid degradation is characterized by complete amino-acid sequence and carbohydrate content. It consists of 79 amino-acid residues and has a molecular mass of 8.875 kDa. The polypeptide chain contains 2 mol of N-acetylglucosamine, bound to asparagine in position 21, as well as 2 mol of galactose and mannose per mol protein. The primary structure of the A2 activator protein is identical to that of the sulfatide activator protein (SAP-1). Possible differences in the carbohydrate content are discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0177-3593
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
369
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1361-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3242555-Amino Acid Sequence,
pubmed-meshheading:3242555-Chromatography, High Pressure Liquid,
pubmed-meshheading:3242555-Female,
pubmed-meshheading:3242555-Gaucher Disease,
pubmed-meshheading:3242555-Glycoproteins,
pubmed-meshheading:3242555-Humans,
pubmed-meshheading:3242555-Middle Aged,
pubmed-meshheading:3242555-Molecular Sequence Data,
pubmed-meshheading:3242555-Peptide Fragments,
pubmed-meshheading:3242555-Saposins,
pubmed-meshheading:3242555-Sphingolipid Activator Proteins,
pubmed-meshheading:3242555-Spleen,
pubmed-meshheading:3242555-Trypsin
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pubmed:year |
1988
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pubmed:articleTitle |
Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1).
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pubmed:affiliation |
Max-Planck-Institut für Biochemie, Martinsried bei München.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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