Accéder au contenu
Merck

The DNA sequence and comparative analysis of human chromosome 10.

Nature (2004-05-28)
P Deloukas, M E Earthrowl, D V Grafham, M Rubenfield, L French, C A Steward, S K Sims, M C Jones, S Searle, C Scott, K Howe, S E Hunt, T D Andrews, J G R Gilbert, D Swarbreck, J L Ashurst, A Taylor, J Battles, C P Bird, R Ainscough, J P Almeida, R I S Ashwell, K D Ambrose, A K Babbage, C L Bagguley, J Bailey, R Banerjee, K Bates, H Beasley, S Bray-Allen, A J Brown, J Y Brown, D C Burford, W Burrill, J Burton, P Cahill, D Camire, N P Carter, J C Chapman, S Y Clark, G Clarke, C M Clee, S Clegg, N Corby, A Coulson, P Dhami, I Dutta, M Dunn, L Faulkner, A Frankish, J A Frankland, P Garner, J Garnett, S Gribble, C Griffiths, R Grocock, E Gustafson, S Hammond, J L Harley, E Hart, P D Heath, T P Ho, B Hopkins, J Horne, P J Howden, E Huckle, C Hynds, C Johnson, D Johnson, A Kana, M Kay, A M Kimberley, J K Kershaw, M Kokkinaki, G K Laird, S Lawlor, H M Lee, D A Leongamornlert, G Laird, C Lloyd, D M Lloyd, J Loveland, J Lovell, S McLaren, K E McLay, A McMurray, M Mashreghi-Mohammadi, L Matthews, S Milne, T Nickerson, M Nguyen, E Overton-Larty, S A Palmer, A V Pearce, A I Peck, S Pelan, B Phillimore, K Porter, C M Rice, A Rogosin, M T Ross, T Sarafidou, H K Sehra, R Shownkeen, C D Skuce, M Smith, L Standring, N Sycamore, J Tester, A Thorpe, W Torcasso, A Tracey, A Tromans, J Tsolas, M Wall, J Walsh, H Wang, K Weinstock, A P West, D L Willey, S L Whitehead, L Wilming, P W Wray, L Young, Y Chen, R C Lovering, N K Moschonas, R Siebert, K Fechtel, D Bentley, R Durbin, T Hubbard, L Doucette-Stamm, S Beck, D R Smith, J Rogers
RÉSUMÉ

The finished sequence of human chromosome 10 comprises a total of 131,666,441 base pairs. It represents 99.4% of the euchromatic DNA and includes one megabase of heterochromatic sequence within the pericentromeric region of the short and long arm of the chromosome. Sequence annotation revealed 1,357 genes, of which 816 are protein coding, and 430 are pseudogenes. We observed widespread occurrence of overlapping coding genes (either strand) and identified 67 antisense transcripts. Our analysis suggests that both inter- and intrachromosomal segmental duplications have impacted on the gene count on chromosome 10. Multispecies comparative analysis indicated that we can readily annotate the protein-coding genes with current resources. We estimate that over 95% of all coding exons were identified in this study. Assessment of single base changes between the human chromosome 10 and chimpanzee sequence revealed nonsense mutations in only 21 coding genes with respect to the human sequence.

MATÉRIAUX
Référence du produit
Marque
Description du produit

Sigma-Aldrich
Lipase from Candida rugosa, Type VII, ≥700 unit/mg solid
Sigma-Aldrich
Lipase from porcine pancreas, Type II, ≥125 units/mg protein (using olive oil (30 min incubation)), 30-90 units/mg protein (using triacetin)
Sigma-Aldrich
Résine acrylique contenant des lipases, ≥5,000 U/g, recombinant, expressed in Aspergillus niger
Sigma-Aldrich
ADN polymérase Taq from Thermus aquaticus, with 10× PCR reaction buffer without MgCl2
Sigma-Aldrich
ADN polymérase Taq from Thermus aquaticus, with 10× PCR reaction buffer containing MgCl2
Sigma-Aldrich
Lipase from porcine pancreas, Type VI-S, ≥20,000 units/mg protein, lyophilized powder
Sigma-Aldrich
Hexokinase from Saccharomyces cerevisiae, Type F-300, lyophilized powder, ≥130 units/mg protein (biuret)
Sigma-Aldrich
Lipase B Candida antarctica, recombinant from Aspergillus oryzae, powder, beige, ~9 U/mg
Sigma-Aldrich
Glutamic-Oxalacetic Transaminase from porcine heart, Type I, ammonium sulfate suspension, 200-500 units/mg protein
Sigma-Aldrich
Lipase from Aspergillus niger, powder (fine), ~200 U/g
Sigma-Aldrich
Lipase from Candida rugosa, lyophilized powder, ≥40,000 units/mg protein
Sigma-Aldrich
Lipase immobilized from Candida antarctica, beads, slightly brown, >2 U/mg
Sigma-Aldrich
Lipase from Candida sp., recombinant, expressed in Aspergillus niger
Sigma-Aldrich
Hexokinase from Saccharomyces cerevisiae, lyophilized powder, ≥350 units/mg protein, Protein ≥10 % by biuret
Sigma-Aldrich
Lipase from Pseudomonas cepacia, powder, light beige, ≥30 U/mg
Sigma-Aldrich
Lipase from Aspergillus oryzae, ≥20,000 U/g
Sigma-Aldrich
Lipase from wheat germ, Type I, lyophilized powder, 5-15 units/mg solid
Sigma-Aldrich
Lipase from Rhizopus oryzae, powder (fine), ~10 U/mg
Sigma-Aldrich
Lipase from Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
Sigma-Aldrich
Lipase from Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
Sigma-Aldrich
Adenosine 5′-Triphosphatase from porcine cerebral cortex, lyophilized powder, ≥0.3 units/mg protein, pH 7.8
Sigma-Aldrich
Lipase from Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
Sigma-Aldrich
Acyl-coenzyme A Synthetase from Pseudomonas sp., ≥2 units/mg protein
Sigma-Aldrich
Lipase from Candida rugosa, powder, yellow-brown, ≥2 U/mg
Sigma-Aldrich
α-Ketoglutarate Dehydrogenase from porcine heart, buffered aqueous glycerol solution, 0.1-1.0 units/mg protein (Lowry)
Sigma-Aldrich
Lipase from Mucor miehei, lyophilized powder, ≥4,000 units/mg solid (using olive oil)
Sigma-Aldrich
Fructose-6-phosphate Kinase from Bacillus stearothermophilus, Type VII, lyophilized powder, ≥50 units/mg protein
Sigma-Aldrich
Lipase from Mucor miehei, powder, slightly brown, ~1 U/mg
Sigma-Aldrich
DNA Polymerase I from Escherichia coli lysogenic for NM 964, buffered aqueous glycerol solution
Sigma-Aldrich
Lipase from Rhizopus niveus, powder (fine), ≥1.5 U/mg