메뉴 건너뛰기




Volumn 27, Issue 1, 2012, Pages 72-74

Human hemoglobin does not contain asymmetric dimethylarginine (ADMA)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; N(G),N(G) DIMETHYLARGININE; PROTEIN HYDROLYSATE;

EID: 84861644821     PISSN: 10898603     EISSN: 10898611     Source Type: Journal    
DOI: 10.1016/j.niox.2012.03.013     Document Type: Letter
Times cited : (8)

References (16)
  • 1
    • 55649118666 scopus 로고    scopus 로고
    • Determination of protein-incorporated methylated arginine reference values in healthy subjects whole blood and evaluation of factors affecting protein methylation
    • A. Zinellu, S. Sotgia, B. Scanu, L. Deiana, and C. Carru Determination of protein-incorporated methylated arginine reference values in healthy subjects whole blood and evaluation of factors affecting protein methylation Clin. Biochem. 41 2008 1218 1223
    • (2008) Clin. Biochem. , vol.41 , pp. 1218-1223
    • Zinellu, A.1    Sotgia, S.2    Scanu, B.3    Deiana, L.4    Carru, C.5
  • 4
    • 77953137357 scopus 로고    scopus 로고
    • Massive quantities of asymmetric dimethylarginine (ADMA) are incorporated in red blood cell proteins and may be released by proteolysis following hemolytic stress
    • L.G. D'Alecy, and S.S. Billecke Massive quantities of asymmetric dimethylarginine (ADMA) are incorporated in red blood cell proteins and may be released by proteolysis following hemolytic stress Blood Cells Mol. Dis. 45 2010 40
    • (2010) Blood Cells Mol. Dis. , vol.45 , pp. 40
    • D'Alecy, L.G.1    Billecke, S.S.2
  • 5
    • 33344456589 scopus 로고    scopus 로고
    • The synthesis and metabolism of asymmetric dimethylarginine (ADMA)
    • J.M. Leiper, and P. Vallance The synthesis and metabolism of asymmetric dimethylarginine (ADMA) Eur. J. Clin. Pharmacol. 26 2006 33 38
    • (2006) Eur. J. Clin. Pharmacol. , vol.26 , pp. 33-38
    • Leiper, J.M.1    Vallance, P.2
  • 6
    • 33344456736 scopus 로고    scopus 로고
    • Asymmetric dimethylarginine (ADMA) and the risk for coronary heart disease. The multicenter CARDIAC study
    • H. Lenzen, D. Tsikas, and R.H. Böger Asymmetric dimethylarginine (ADMA) and the risk for coronary heart disease. The multicenter CARDIAC study Eur. J. Clin. Pharmacol. 62 2006 45 49
    • (2006) Eur. J. Clin. Pharmacol. , vol.62 , pp. 45-49
    • Lenzen, H.1    Tsikas, D.2    Böger, R.H.3
  • 7
    • 0342757751 scopus 로고    scopus 로고
    • Endogenous nitric oxide synthase inhibitors are responsible for the L-arginine paradox
    • D. Tsikas, R.H. Böger, J. Sandmann, S.M. Bode-Böger, and J.C. Frölich Endogenous nitric oxide synthase inhibitors are responsible for the L-arginine paradox FEBS Lett. 478 2000 1 3
    • (2000) FEBS Lett. , vol.478 , pp. 1-3
    • Tsikas, D.1    Böger, R.H.2    Sandmann, J.3    Bode-Böger, S.M.4    Frölich, J.C.5
  • 8
    • 34248224898 scopus 로고    scopus 로고
    • A stable-isotope based technique for the determination of dimethylarginine dimethylaminohydrolase (DDAH) activity in mouse tissue
    • R. Maas, J. Tan-Andreesen, E. Schwedhelm, F. Schulze, and R.H. Böger A stable-isotope based technique for the determination of dimethylarginine dimethylaminohydrolase (DDAH) activity in mouse tissue J. Chromatogr. B 851 2007 220 228
    • (2007) J. Chromatogr. B , vol.851 , pp. 220-228
    • Maas, R.1    Tan-Andreesen, J.2    Schwedhelm, E.3    Schulze, F.4    Böger, R.H.5
  • 9
    • 70349764307 scopus 로고    scopus 로고
    • Albumin from human serum does not contain asymmetric dimethylarginine (ADMA)
    • D. Tsikas, and B. Beckmann Albumin from human serum does not contain asymmetric dimethylarginine (ADMA) Clin. Biochem. 42 2009 1739 1740
    • (2009) Clin. Biochem. , vol.42 , pp. 1739-1740
    • Tsikas, D.1    Beckmann, B.2
  • 10
    • 77949917115 scopus 로고    scopus 로고
    • Asymmetric dimethylarginine (ADMA) is present in plasma proteins of healthy subjects at the low nmol-per-g-level
    • D. Tsikas, S. Engeli, B. Beckmann, and J. Jordan Asymmetric dimethylarginine (ADMA) is present in plasma proteins of healthy subjects at the low nmol-per-g-level Nitric Oxide 22 2010 316 317
    • (2010) Nitric Oxide , vol.22 , pp. 316-317
    • Tsikas, D.1    Engeli, S.2    Beckmann, B.3    Jordan, J.4
  • 11
    • 37149042523 scopus 로고    scopus 로고
    • Assessment of protein-incorporated arginine methylation in biological specimens by CZE UV-detection
    • A. Zinellu, S. Sotgia, B. Scanu, M. Formato, L. Deiana, and C. Carru Assessment of protein-incorporated arginine methylation in biological specimens by CZE UV-detection Electrophoresis 28 2007 4452 4458
    • (2007) Electrophoresis , vol.28 , pp. 4452-4458
    • Zinellu, A.1    Sotgia, S.2    Scanu, B.3    Formato, M.4    Deiana, L.5    Carru, C.6
  • 12
    • 0242412270 scopus 로고    scopus 로고
    • Quantitative determination of circulating and urinary asymmetric dimethylarginine (ADMA) in humans by gas chromatography-tandem mass spectrometry as methyl ester tri(N-pentafluoropropionyl) derivative
    • D. Tsikas, B. Schubert, F.M. Gutzki, J. Sandmann, and E. Schwedhelm Quantitative determination of circulating and urinary asymmetric dimethylarginine (ADMA) in humans by gas chromatography-tandem mass spectrometry as methyl ester tri(N-pentafluoropropionyl) derivative J. Chromatogr. B 798 2003 87 99
    • (2003) J. Chromatogr. B , vol.798 , pp. 87-99
    • Tsikas, D.1    Schubert, B.2    Gutzki, F.M.3    Sandmann, J.4    Schwedhelm, E.5
  • 13
    • 36148933356 scopus 로고    scopus 로고
    • Sensitivity enhancement of a GC-MS/MS method for asymmetric dimethylarginine (ADMA) by plasma ultrafiltrate reduction
    • B. Beckmann, F.M. Gutzki, and D. Tsikas Sensitivity enhancement of a GC-MS/MS method for asymmetric dimethylarginine (ADMA) by plasma ultrafiltrate reduction Anal. Biochem. 372 2 2008 264 266
    • (2008) Anal. Biochem. , vol.372 , Issue.2 , pp. 264-266
    • Beckmann, B.1    Gutzki, F.M.2    Tsikas, D.3
  • 14
    • 33750616737 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis
    • N. Bader, and T. Grune Protein oxidation and proteolysis Biol. Chem. 387 2006 1351 1355
    • (2006) Biol. Chem. , vol.387 , pp. 1351-1355
    • Bader, N.1    Grune, T.2
  • 15
    • 79551560227 scopus 로고    scopus 로고
    • High-performance liquid chromatography ultraviolet assay for human erythrocytic catalase activity by measuring glutathione as o-phthalaldehyde derivative
    • A. Böhmer, J. Jordan, and D. Tsikas High-performance liquid chromatography ultraviolet assay for human erythrocytic catalase activity by measuring glutathione as o-phthalaldehyde derivative Anal. Biochem. 410 2011 296 303
    • (2011) Anal. Biochem. , vol.410 , pp. 296-303
    • Böhmer, A.1    Jordan, J.2    Tsikas, D.3
  • 16
    • 0015034950 scopus 로고
    • Methyltransferase enzyme in red blood cells
    • J. Axelrod, and C.K. Cohn Methyltransferase enzyme in red blood cells J. Pharmacol. Exp. Ther. 176 1971 650 654
    • (1971) J. Pharmacol. Exp. Ther. , vol.176 , pp. 650-654
    • Axelrod, J.1    Cohn, C.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.