Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1976-1-2
pubmed:abstractText
We have been able to purify, in bulk, the cytoplasmic microtubule proteins of eggs and embryos of Drosophila melanogaster by means of in vitro self-assembly of microtubules from subunits present in a high-speed supernatant fraction of eggs or embryos. This provides the first successful application of this method to purification of microtubule protein from a source other than vertebrate brain, and the first purification of insect microtubule proteins. Our electron micrographs show that the in vitro assembled microtubules are morphologically typical and apparently are comprised of the expected 13 protofilaments. The protein we obtain from such preparations binds [3H]colchicine and has a sedimentation value of 6.4 S-6.9 S which is close to the predicted value for microtubule protein dimer. Both alpha- and beta-microtubule proteins are evident in sodium dodecyl sulfate polyacrylamide electropherograms of the isolated proteins. The apparent molecular weights of these species on dodecyl sulfate polyacrylamide gels are 54,000 and 52,000, respectively. These values as well as the amino acid composition and N-terminal methionine of the Drosophilia proteins are very closely comparable to microtubule proteins from other, unrelated organisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4487-91
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Cytoplasmic microtubule proteins of the embryo of Drosophila melanogaster.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.