Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-3-24
pubmed:abstractText
We have studied the membrane topography of N-acetylneuraminic acid (NeuAc) in sialoglycoproteins of mouse and rat liver Golgi apparatus vesicles. Purified Golgi vesicles or Golgi vesicles present in microsomes were able to incorporate radiolabeled NeuAc from CMP-NeuAc into endogenous glycoproteins in vitro. The labeled glycoproteins showed a similar profile on sodium dodecyl sulfate gel electrophoresis to those isolated from Golgi fractions of animals injected with radiolabeled NeuAc. Using this labeling procedure in vitro, we found that only 5 to 20% of the incorporated NeuAc could be removed from intact vesicles upon treatment with neuraminidase or proteases. However, disruption of vesicles by detergents or mechanical means prior to the enzymatic treatments resulted in removal of labeled NeuAc; the extent of NeuAc removal could be correlated with that of vesicle disruption as measured by loss of latency of thiamine pyrophosphatase activity. This strongly suggests that NeuAc residues of glycoproteins are on the lumenal side of the Golgi apparatus membrane and that Golgi-derived vesicles have the same membrane orientation as in vivo. A similar approach was used to infer a lumenal orientation of sialyltransferases. Not all Golgi apparatus preparations routinely used may be suitable for membrane topography experiments of the kind described here.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
989-93
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Topography of sialoglycoproteins and sialyltransferases in mouse and rat liver Golgi.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't