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A comparison of 18s ribosomal RNA and rubisco large subunit sequences for studying angiosperm phylogeny (1991)

Martin, P. G. ; Dowd, J. M.

Springer

Journal of molecular evolution 33 (1991), S. 274-282

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ISSN: 1432-1432

Keywords: Angiosperm phylogeny ; 18s rRNA sequences ; Rubisco large subunit sequences ; Leaf RNA preparation ; Chloroplast DNA variation ; Base composition

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Partial sequences of 18s rRNA were obtained for 2 gymnosperms and 12 angiosperms from a wide range of families and these were analyzed with 5 other published sequences to form a phylogenetic tree. Using 16 published sequences of the large subunit of rubisco (rbcL), also from a wide range of angiosperm families, another phylogenetic tree was derived and the two approaches were compared. Both phylogenetic trees gave good grouping within families but in neither case was there resolution of the branching order of major taxa. Superficially the long rbcL sequences (whose base composition was homogeneous among all species) seemed very promising, but analysis showed that a large proportion of the variation did not affect the amino acid sequence. Although silent substitution contained some phylogenetic information, at the level required to order major taxa, much of it was random and obfuscating. It was concluded that neither macromolecule alone was likely to yield a solution to the problem of angiosperm phylogeny and therefore that studies of both, at least, will be required. For this reason, a method wa described for obtaining both DNA and RNA of good quality from the same preparation and which had been used successfully with a wide range of species including many with pungent leaves.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02100679

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Heterotrimeric configuration is essential to the adhesive function of laminin (1992)

Lissitzky, J. C. ; Cantau, P. ; Martin, P. M.

New York, N.Y. : Wiley-Blackwell

Journal of Cellular Biochemistry 48 (1992), S. 141-149

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ISSN: 0730-2312

Keywords: laminin ; structure-function ; adhesion ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: Mouse PFHR9 laminin, B1B2-heterodimers, and free B1-chains were separated from one another by gel filtration on superose 6. The cell attachment promoting activity of these species was measured after immunoprecipitation with monoclonal anti-laminin antibodies coupled to Sepharose 6MB beads. These antibodies, Which did not react with the laminin E8 fragment, were directed against epitopes in the NH2-terminus of the laminin B1-chain and in the central region of laminin. After incubation with purified EHS laminin, the immunosorbents revealed efficient adhesion substrates for a rat rhabdomyosarcoma cell line which attached preferentially to the laminin E8 fragment. Although both were immunoprecipitated efficiently, B1B2-heterodimers and B1-chains, unlike PFHR9 laminin, did not support the attachment of RMS cells. On a molar basis B1B2-heterodimers were 24 times less efficient than PFHR9 laminin or EHS laminin in supporting cell attachment. These data suggest that heterotrimeric configuration is essential to the adhesive function of the laminin E8 fragment.

Additional Material: 5 Ill.