Linked Life Data

6480399

Source:http://linkedlifedata.com/resource/pubmed/id/6480399

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1984-11-21
pubmed:abstractText
The acid hydrolases alpha-glucosidase, beta-galactosidase, N-acetyl-beta-D-hexosaminidase, beta-glucocerebrosidase and cathepsin D were studied immunocytochemically in normal and mutant human cells using monoclonal and affinity-purified polyclonal antibodies. For light microscopy, Rhodamine or Fluorescein-labelled conjugates were used, and for electron microscopy protein A-gold conjugates were employed. With the double labelling procedure, it was found that in normal fibroblasts every lysosome contained all the enzymes studied. The method described also enabled us to demonstrate the presence or absence of mutant enzyme protein in fibroblasts derived from patients with a genetic lysosomal enzyme deficiency. Immunoreactive acid hydrolases or their precursor forms were found in the rough endoplasmic reticulum, the cisternae of the Golgi complex, Golgi associated vesicles and lysosomes. This is in agreement with the present concept that the Golgi complex plays an essential role in the processing and targeting of lysosomal enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0018-2214
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
941-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Immunocytochemistry of lysosomal hydrolases and their precursor forms in normal and mutant human cells.
pubmed:publicationType
Journal Article, Comparative Study