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Deoxyribonucleic acid (DNA) polymorphism of the alpha 1-antitrypsin gene in chronic lung disease. 원문보기

British medical journal, v.294 no.6586 = no.6586, 1987년, pp.1511 - 1514  

Kalsheker, N A ,  Hodgson, I J ,  Watkins, G L ,  White, J P ,  Morrison, H M ,  Stockley, R A

Abstract AI-Helper 아이콘AI-Helper

Specific gene probes were used to study restriction fragment length polymorphisms of the human alpha 1-antitrypsin gene. A polymorphism due to loss of a recognition site for the restriction enzyme Taq I was identified in eight of 42 patients with bronchiectasis and nine of 49 patients with pulmonary...

참고문헌 (29)

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  6. 1987 (Accepted 23 March 1987) 

  7. Specific gene probes were used to study restriction fragment length polymorphisms of the human a1-antitrypsin gene. A polymorphism due to loss of a recognition site for the restriction enzyme Taq I was identified in eight of 42 patients with bronchiectasis and nine of 49 patients with pulmonary emphysema, none of whom had a1-antitrypsin deficiency. Among a control group without lung disease the polymorphism was significantly less frequent, being found in only five of 101 apparently healthy blood donors. The deoxyribonucleic acid (DNA) polymorphism was also present in two of 14 unrelated patients with a1-antitrypsin deficiency, indicating a lack of association with any specific a I-antitrypsin protein phenotype Specific gene probes were used to study restriction fragment length polymorphisms of the human a1-antitrypsin gene. A polymorphism due to loss of a recognition site for the restriction enzyme Taq I was identified in eight of 42 patients with bronchiectasis and nine of 49 patients with pulmonary emphysema, none of whom had a1-antitrypsin deficiency. Among a control group without lung disease the polymorphism was significantly less frequent, being found in only five of 101 apparently healthy blood donors. The deoxyribonucleic acid (DNA) polymorphism was also present in two of 14 unrelated patients with a1-antitrypsin deficiency, indicating a lack of association with any specific a I-antitrypsin protein phenotype. 

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  11. Tobin, M.J.; Cook, P.J.L.; Hutchinson, D.C.S. Alpha1-antitrypsin deficiency; the clinical and physiological features of pulmonary emphysema in subjects homozygous for Pi type Z. BrJ Dis Chest 1983 10.1016/0007-0971(83)90002-5 77 14 Tobin MJ, Cook PJL, Hutchinson DCS. Alpha1-antitrypsin deficiency; the clinical and physiological features of pulmonary emphysema in subjects homozygous for Pi type Z. BrJ Dis Chest 1983;77:14-27. 

  12. Mittman, C.; Barbella, T.; Lieberman, J. Alphat-antitrypsin deficiency as an indicator of susceptibility to pulmonary disease J7 Occup Med 1973 15 33 Mittman C, Barbella T, Lieberman J. Alphat-antitrypsin deficiency as an indicator of susceptibility to pulmonary disease. J7 Occup Med 1973;15:33-8. 

  13. Hodgson, I.; Kalsheker, N. DNA polymorphisms of the human alpha,-antitrypsin (AAT) gene in normal subjects and in patients with pulmonary emphysema J Med Genet 1987 10.1136/jmg.24.1.47 24 47 Hodgson I, Kalsheker N. DNA polymorphisms of the human alpha,-antitrypsin (AAT) gene in normal subjects and in patients with pulmonary emphysema. J Med Genet 1987;24:47-51. 

  14. Long, G.L.; Chandra, T.; Woo, S.L.C.; Davie, E.W.; Kurachi, K. Complete sequence of the cDNA for human alphat-antitrypsin and the gene for the S variant Biochemistry 1984 10.1021/bi00316a003 23 4828 Long GL, Chandra T, Woo SLC, Davie EW, Kurachi K. Complete sequence of the cDNA for human alphat-antitrypsin and the gene for the S variant. Biochemistry 1984;23:4828-37. 

  15. Rogers, J.; Kalsheker, N.; Wallis, S. The isolation of a clone for human al-antitrypsin and the detection of al-antitrypsin in inRNA from liver and leukocytes Biochem Biophys Res Commun 1983 10.1016/0006-291X(83)90532-6 116 375 Rogers J, Kalsheker N, Wallis S, et al. The isolation of a clone for human al-antitrypsin and the detection of al-antitrypsin in inRNA from liver and leukocytes. Biochem Biophys Res Commun 1983;116:375-82. 

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  17. Southern, E.M. Detection of specific sequences among DNA fragments separated by gel electrophoresis J MolBiol 1975 10.1016/S0022-2836(75)80083-0 98 503 Southern EM. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J MolBiol 1975;98:503-17. 

  18. Qureshi, A.R.; Punnett, H.H. An improved method for phenotyping of alpha1-antitrypsin variants using separator isoelectric focusing on thin layer agarose gel Anal Biochem 1982 10.1016/0003-2697(82)90014-8 125 335 Qureshi AR, Punnett HH. An improved method for phenotyping of alpha1-antitrypsin variants using separator isoelectric focusing on thin layer agarose gel. Anal Biochem 1982;125:335-8. 

  19. Klumpp, T.; Bieth, J.G. Automated measurement of the elastase-inhibitor capacity of plasma with a centrifugal analyser Clin Chem 1979 10.1093/clinchem/25.6.969 25 969 Klumpp T, Bieth JG. Automated measurement of the elastase-inhibitor capacity of plasma with a centrifugal analyser. Clin Chem 1979;25:969-72. 

  20. Cox, D.W.; Woo, S.L.C.; Mansfield, T. DNA restriction fragments associated with al-antitrypsin indicate a single origin for deficiency allele Pi Z. Nature 1985 10.1038/316079a0 316 79 Cox DW, Woo SLC, Mansfield T. DNA restriction fragments associated with al-antitrypsin indicate a single origin for deficiency allele, Pi Z. Nature 1985;316:79-81. 

  21. al-Antitrypsin. In, Milford Ward A. in clinical laboratowy medicine 1979 183 Milford Ward A. al-Antitrypsin. In: Milford Ward A, Whicher JT, eds. Immunochemistry in clinical laboratowy medicine. Lancaster: MTP Press, 1979:183-95. 

  22. Matteson, H.J.; Ostrer, H.; Chakravarti, A. A study of restriction fragment length polymorphisms at the human alphat-antitrypsin locus Hum Genet 1985 10.1007/BF00293037 69 263 Matteson HJ, Ostrer H, Chakravarti A, et al. A study of restriction fragment length polymorphisms at the human alphat-antitrypsin locus. Hum Genet 1985;69:263-7. 

  23. Brantly, M.; Paul, L.; Strauss, S. Heterogeneity of al-antitrypsin gene sequences among individuals with the M phenotype Clin Res 1984 32 288 Brantly M, Paul L, Strauss S, et al. Heterogeneity of al-antitrypsin gene sequences among individuals with the M phenotype. Clin Res 1984;32:A288. 

  24. Lai, E.C.; Kao, F.T.; Law, M.L.; Woo, S.L.C. Assignment of the alphat-antitrypsin and a sequence related gene to human chromosome 14 by molecular hybridisation Am J Hum Genet 1983 35 385 Lai EC, Kao FT, Law ML, Woo SLC. Assignment of the alphat-antitrypsin and a sequence related gene to human chromosome 14 by molecular hybridisation. Am J Hum Genet 1983;35:385-92. 

  25. Rabin, M.; Watson, M.; Kidd, V.; Woo, S.L.C.; Breg, W.R.; Ruddle, F.H. Regional location of al-antichymotrypsin and al-antitrypsin genes on human chromosome 14 Somatic Cell Mol Genet 1986 10.1007/BF01560668 12 209 Rabin M, Watson M, Kidd V, Woo SLC, Breg WR, Ruddle FH. Regional location of al-antichymotrypsin and al-antitrypsin genes on human chromosome 14. Somatic Cell Mol Genet 1986;12:209-14. 

  26. Stockley, R.A. Proteolytic enzymes, their inhibitors and lung disease Clin Sci 1983 10.1042/cs0640119 64 119 Stockley RA. Proteolytic enzymes, their inhibitors and lung disease. Clin Sci 1983;64:119-26. 

  27. Jones, D.K.; Gaddon, D.; Cavanagh, P. Alpha-l-antitrypsin deficiency presenting as bronchiectasis BrJ Dis Chest 1985 79 3014 Jones DK, Gaddon D, Cavanagh P. Alpha-l-antitrypsin deficiency presenting as bronchiectasis. BrJ Dis Chest 1985;79:3014. 

  28. Cotes, J.E. Lung function throughout life: determinants and reference values. Lutig function assessment and applications in medicine 3rd ed 1975 386 Cotes JE. Lung function throughout life: determinants and reference values. Lutig function assessment and applications in medicine. 3rd ed. Oxiord: Blackwell Scientific, 1975:386-7. 

  29. Accepted 15 1987 (Accepted 15 April 1987) 

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