Linked Life Data

4006900

Source:http://linkedlifedata.com/resource/pubmed/id/4006900

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-8-20
pubmed:abstractText
The biosynthesis of alpha-N-acetylglucosaminidase was studied in cultured human kidney carcinoma cells by labeling cells with 35S-methionine, isolation of the enzyme by immunoprecipitation and analysis on gel electrophoresis of the denatured polypeptide(s) and analysis of the native enzyme on linear sucrose gradient centrifugation. The enzyme is synthesized as precursor forms of apparent molecular weight 82,000-86,000. Processing of these precursors yields a polypeptide of apparent molecular weight of 80,000. The precursor-product relationship was indicated by pulse-chase as well as endocytosis experiments. Sucrose gradient centrifugation of the native enzyme shows that, extracellularly, the molecule is present with a molecular weight of 80,000; intracellularly, 80-90% of the enzyme is present with an apparent molecular weight of 240,000. We suggest that this is a polymeric form and that polymerization of alpha-N-acetylglucosaminidase is a late event of the maturation process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0013-9432
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
75-83
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Biosynthesis of alpha-N-acetylglucosaminidase in cultured human kidney carcinoma cells.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't