pubmed-article:3084715 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C0027882 | lld:lifeskim |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C0010852 | lld:lifeskim |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:3084715 | lifeskim:mentions | umls-concept:C1272706 | lld:lifeskim |
pubmed-article:3084715 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:3084715 | pubmed:dateCreated | 1986-6-6 | lld:pubmed |
pubmed-article:3084715 | pubmed:abstractText | We have used pulse-chase experiments to study the time interval between the synthesis and assembly of tubulin and neurofilament proteins (NFP) in sympathetic neurons grown in tissue culture. After varying pulse-chase times, cultures were extracted with Triton X-100 such that polymerized tubulin and NFP were insoluble, while unassembled tubulin and NFP were quantitatively solubilized. The partitioning of labeled tubulin and NFP between Triton X-100-soluble and insoluble, or cytoskeletal, fractions was determined with an isoelectric focusing X SDS gel electrophoresis assay. Labeled tubulin and NFP in cultures pulse-labeled for 5-10 min partitions primarily with the soluble fraction. When pulse-labeled cultures were chased for increasing periods of time, relatively more of the total labeled tubulin and NFP partitioned with the cytoskeleton, attaining maximal values after chase times of 60-120 and 15-30 min, respectively. The maximal values for the relative levels of labeled tubulin and NFP in polymer were 70-75 and greater than 90%, respectively. The levels of labeled tubulin and NFP synthesized during a short pulse-label remained constant for at least 2 hr, indicating that selective turnover of soluble tubulin and NFP does not detectably contribute to the changes in solubility properties of these proteins observed in the pulse-chase experiments. These results indicate that newly synthesized tubulin and NFP are rapidly assembled from soluble precursors. The lag between the synthesis and assembly of the 145,000-molecular-weight NFP is not related to its phosphorylation because its initial incorporation into the cytoskeleton occurs prior to its phosphorylation.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
pubmed-article:3084715 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3084715 | pubmed:language | eng | lld:pubmed |
pubmed-article:3084715 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3084715 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3084715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:3084715 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3084715 | pubmed:month | Apr | lld:pubmed |
pubmed-article:3084715 | pubmed:issn | 0270-6474 | lld:pubmed |
pubmed-article:3084715 | pubmed:author | pubmed-author:BlackM MMM | lld:pubmed |
pubmed-article:3084715 | pubmed:author | pubmed-author:SobelEE | lld:pubmed |
pubmed-article:3084715 | pubmed:author | pubmed-author:KeyserPP | lld:pubmed |
pubmed-article:3084715 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3084715 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:3084715 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3084715 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3084715 | pubmed:pagination | 1004-12 | lld:pubmed |
pubmed-article:3084715 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:3084715 | pubmed:meshHeading | pubmed-meshheading:3084715-... | lld:pubmed |
pubmed-article:3084715 | pubmed:year | 1986 | lld:pubmed |
pubmed-article:3084715 | pubmed:articleTitle | Interval between the synthesis and assembly of cytoskeletal proteins in cultured neurons. | lld:pubmed |
pubmed-article:3084715 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3084715 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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