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L773:0300 8177 OR L773:1573 4919
 

Sökning: L773:0300 8177 OR L773:1573 4919 > (1991-1994) > Dependency of micro...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003476naa a2200505 4500
001oai:gup.ub.gu.se/114023
003SwePub
008240528s1991 | |||||||||||000 ||eng|
024a https://gup.ub.gu.se/publication/1140232 URI
040 a (SwePub)gu
041 a eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Fridén, Bu Gothenburg University,Göteborgs universitet,Zoologiska institutionen,Department of Zoology4 aut
2451 0a Dependency of microtubule-associated proteins (MAPs) for tubulin stability and assembly; use of estramustine phosphate in the study of microtubules.
264 1c 1991
520 a Microtubule-associated proteins (MAPs) were separated from tubulin with several different methods. The ability of the isolated MAPs to reinduce assembly of phosphocellulose purified tubulin differed markedly between the different methods. MAPs isolated by addition of 0.35 M NaCl to taxol-stabilized microtubules stimulated tubulin assembly most effectively, while addition of 0.6 M NaCl produced MAPs with a substantially lower ability to stimulate tubulin assembly. The second best preparation was achieved with phosphocellulose chromatographic separation of MAPs with 0.6 M NaCl elution. The addition of estramustine phosphate to microtubules reconstituted of MAPs prepared by 0.35 M NaCl or phosphocellulose chromatography, induced less disassembly than for microtubules assembled from unseparated proteins, and was almost without effect on microtubules reconstituted from MAPs prepared by taxol and 0.6 M NaCl. Estramustine phosphate binds to the tubulin binding part of the MAPs, and the results do therefore indicate that the MAPs are altered by the separation methods. Since the MAPs are regarded as highly stable molecules, one probable alteration could be aggregation of the MAPs, as also indicated by the results. The purified tubulin itself seemed not to be affected by the phosphocellulose purification, since the microtubule proteins were unchanged by the low buffer strenght used during the cromatography. However, the assembly competence after a prolonged incubation of the microtubule proteins at 4 degrees C was dependent on intact bindings between the tubulin and MAPs.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653 a Alkaloids
653 a pharmacology
653 a Animals
653 a Brain Chemistry
653 a Cattle
653 a Electrophoresis
653 a Polyacrylamide Gel
653 a Estramustine
653 a metabolism
653 a pharmacology
653 a Microtubule-Associated Proteins
653 a chemistry
653 a isolation & purification
653 a metabolism
653 a Microtubules
653 a chemistry
653 a drug effects
653 a ultrastructure
653 a Paclitaxel
653 a Tubulin
653 a metabolism
700a Wallin, Margareta,d 1952u Gothenburg University,Göteborgs universitet,Zoologiska institutionen,Department of Zoology4 aut0 (Swepub:gu)xwmars
710a Göteborgs universitetb Zoologiska institutionen4 org
773t Molecular and cellular biochemistryg 105:2, s. 149-58q 105:2<149-58x 0300-8177
8564 8u https://gup.ub.gu.se/publication/114023

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