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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-12-4
pubmed:abstractText
The occurrence and subcellular distribution of the non-specific lipid transfer protein (nsL-TP; sterol carrier protein 2) in rat tissues was investigated by the immunoblotting technique using the affinity purified antibody against rat liver nsL-TP. Highest levels of the protein were found in the homogenates of liver, lung and adrenals, whereas it could hardly be detected in brain. In other tissues (i.e., testis, kidney, heart and intestine) the protein was present at intermediate concentrations. Analysis of subcellular fractions obtained by differential centrifugation demonstrated that in all tissues except for the liver, nsL-TP was predominantly present in the particulate fractions. In the particulate fractions of all tissues, an immunoreactive 58 kDa-protein was detected. Density centrifugation of a nuclear-free homogenate from liver and testis indicated that the 58 kDa-protein did, and nsL-TP did not, cofractionate with catalase. This suggests that in these tissues the bulk of nsL-TP is extraperoxisomal. Membrane-bound nsL-TP in testis was sensitive to trypsin treatment, suggesting that it is exposed to the cytosol. Release of nsL-TP by washing the membranes with 0.1 M Na2CO3 (pH 11.5), indicated that nsL-TP is a periferal protein. It was shown by chromatofocussing that nsL-TP extracted from membrane fractions was more basic than nsL-TP present in the cytosol fraction from rat liver (isoelectric point of 8.7).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
1046
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
315-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
The occurrence of soluble and membrane-bound non-specific lipid transfer protein (sterol carrier protein 2) in rat tissues.
pubmed:affiliation
Centre for Biomembranes and Lipid Enzymology, State University of Utrecht, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't