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  • 1
    ISSN: 1573-6857
    Keywords: Didelphidae ; FISH ; karyotype evolution ; marsupials ; (T2AG3)ntelomeric sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract It has been suggested that the karyotype of the marsupials derived from a low diploid number (2n = 14) which originated, through fissions of biarmed chromosomes, the karyotypes with a higher 2n. The telomeric sequence (T2AG3)nwas in situhybridized to the chromosomes of Gracilinanus microtarsusand G. emiliae, Micoureus demeraraeand Marmosa murina, species with 2n = 14, in Monodelphissp., M. domestica, M. kunsiand M. brevicaudatawith 2n = 18, and in Lutreolina crassicaudata, Didelphis albiventris, Chironectes minimus, Philander opossumand P. frenata, all of them with 2n = 22. The probe hybridization occurred in the telomeric regions of both arms, short and long, of all chromosomes of the complement of all individuals of all species analysed. However, in some pairs of the karyotypes of Gracilinanus microtarsusand Micoureus demerarae(with 2n = 14), and in Monodelphissp., M. domestica, M. kunsiand M. brevicaudata(2n = 18) ectopic signs of hybridization were detected proximal to the centromeres, suggesting the retention of this telomeric sequence in the centromeric regions of some chromosomes of these species. Based on these results, it is proposed that the karyotype of marsupials evolved from a 2n = 22 to a 2n = 14, by means of chromosomal fusions.
    Type of Medium: Electronic Resource
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2008-07-16
    Description: Many cellular reactions involve both hydrophobic and hydrophilic molecules that reside within the chemically distinct environments defined by the phospholipid-based membranes and the aqueous lumens of cytoplasm and organelles. Enzymes performing this type of reaction are required to access a lipophilic substrate located in the membranes and to catalyze its reaction with a polar, water-soluble compound. Here, we explore the different binding strategies and chemical tricks that enzymes have developed to overcome this problem. These reactions can be catalyzed by integral membrane proteins that channel a hydrophilic molecule into their active site, as well as by water-soluble enzymes that are able to capture a lipophilic substrate from the phospholipid bilayer. Many chemical and biological aspects of this type of enzymology remain to be investigated and will require the integration of protein chemistry with membrane biology.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Forneris, Federico -- Mattevi, Andrea -- New York, N.Y. -- Science. 2008 Jul 11;321(5886):213-6. doi: 10.1126/science.1151118.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, 27100 Pavia, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18621661" target="_blank"〉PubMed〈/a〉
    Keywords: Alkyl and Aryl Transferases/chemistry/metabolism ; Amidohydrolases/chemistry/metabolism ; Binding Sites ; Catalytic Domain ; Cytosol/enzymology/metabolism ; Diffusion ; Enzymes/*chemistry/*metabolism ; Hydrophobic and Hydrophilic Interactions ; Hydroxysteroid Dehydrogenases/chemistry/metabolism ; Intracellular Membranes/enzymology/*metabolism ; Lipid Bilayers/*metabolism ; Membrane Proteins/chemistry/*metabolism ; Metalloproteases/chemistry/metabolism ; Models, Chemical ; Organelles/enzymology/*metabolism ; Peptidoglycan Glycosyltransferase/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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