메뉴 건너뛰기




Volumn 52, Issue 3, 1996, Pages 401-406

Differential distribution of free and bound glutathione and cyst(e)ine in human blood

Author keywords

cyst(e)ine; erythrocytes; free and bound; glutathione; human blood; plasma

Indexed keywords

CYSTEINE; CYSTINE; GLUTATHIONE;

EID: 0030576641     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/0006-2952(96)00241-9     Document Type: Article
Times cited : (111)

References (60)
  • 1
    • 0018195287 scopus 로고
    • The glutathione status of cells
    • 1. Kosower NS and Kosower EM, The glutathione status of cells. Int Rev Cytol 54: 109-160, 1978.
    • (1978) Int Rev Cytol , vol.54 , pp. 109-160
    • Kosower, N.S.1    Kosower, E.M.2
  • 2
    • 0012074243 scopus 로고
    • Manifestations of changes in the G-SH-G-S-S-G status of biological systems
    • Eds. Flohé L, Benöhr HCh, Sies H, Waller HD and Wendel A, Academic Press, New York
    • 2. Kosower EM and Kosower NS, Manifestations of changes in the G-SH-G-S-S-G status of biological systems. In: Glutathione (Eds. Flohé L, Benöhr HCh, Sies H, Waller HD and Wendel A), pp. 287-297. Academic Press, New York, 1974.
    • (1974) Glutathione , pp. 287-297
    • Kosower, E.M.1    Kosower, N.S.2
  • 3
    • 0023257040 scopus 로고
    • The determination of glutathione, cyst(e)ine and other thiols and disulfides in biological samples using high-performance liquid chromatography and dual electrochemical detection
    • 3. Richte JP Jr and Lang CA, The determination of glutathione, cyst(e)ine and other thiols and disulfides in biological samples using high-performance liquid chromatography and dual electrochemical detection. Anal Biochem 163: 9-15, 1986.
    • (1986) Anal Biochem , vol.163 , pp. 9-15
    • Richte J.P., Jr.1    Lang, C.A.2
  • 5
    • 0028033081 scopus 로고
    • Glutathione disulfide variability in normal human blood
    • 5. Mills BJ, Richie JP Jr and Lang CA, Glutathione disulfide variability in normal human blood. Anal Biochem 222: 95-101, 1994.
    • (1994) Anal Biochem , vol.222 , pp. 95-101
    • Mills, B.J.1    Richie J.P., Jr.2    Lang, C.A.3
  • 6
    • 0000851342 scopus 로고
    • The free amino acids of human blood plasma
    • 6. Stein WH and Moore S, The free amino acids of human blood plasma. J Biol Chem 211: 915-926, 1954.
    • (1954) J Biol Chem , vol.211 , pp. 915-926
    • Stein, W.H.1    Moore, S.2
  • 7
    • 0012079604 scopus 로고
    • The reversible binding of half-cystine residues to serum protein, and its bearing on the cystine requirement of cultured mammalian cells
    • 7. Eagle H, Oyama VI and Piez KA, The reversible binding of half-cystine residues to serum protein, and its bearing on the cystine requirement of cultured mammalian cells. J Biol Chem 235: 1719-1726, 1960.
    • (1960) J Biol Chem , vol.235 , pp. 1719-1726
    • Eagle, H.1    Oyama, V.I.2    Piez, K.A.3
  • 8
    • 0017339770 scopus 로고
    • Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue
    • 8. Isaacs J and Binkley F, Glutathione dependent control of protein disulfide-sulfhydryl content by subcellular fractions of hepatic tissue. Biochim Biophys Acta 497: 192-204, 1977.
    • (1977) Biochim Biophys Acta , vol.497 , pp. 192-204
    • Isaacs, J.1    Binkley, F.2
  • 9
    • 0016670923 scopus 로고
    • Ozone interaction with rodent lung. III. Oxidation of reduced glutathione and formation of mixed disulfides between protein and nonprotein sulfhydryls
    • 9. DeLucia AJ, Mustafa MG, Hussain MZ and Cross CE, Ozone interaction with rodent lung. III. Oxidation of reduced glutathione and formation of mixed disulfides between protein and nonprotein sulfhydryls. J Clin Invest 55: 794-802, 1975.
    • (1975) J Clin Invest , vol.55 , pp. 794-802
    • Delucia, A.J.1    Mustafa, M.G.2    Hussain, M.Z.3    Cross, C.E.4
  • 10
    • 0019935286 scopus 로고
    • The formation of mixed disulfides in rat lung following paraquat administration
    • 10. Keeling PL, Smith LL and Aldridge WN, The formation of mixed disulfides in rat lung following paraquat administration. Biochim Biophys Acta 716: 249-257, 1982.
    • (1982) Biochim Biophys Acta , vol.716 , pp. 249-257
    • Keeling, P.L.1    Smith, L.L.2    Aldridge, W.N.3
  • 11
    • 0020025906 scopus 로고
    • Increase in hepatic mixed disulfides and glutathione levels elicited by paraquat
    • 11. Brigelius R, Lenzen R and Sies H, Increase in hepatic mixed disulfides and glutathione levels elicited by paraquat. Biochem Pharmacol 31: 1637-1641, 1982.
    • (1982) Biochem Pharmacol , vol.31 , pp. 1637-1641
    • Brigelius, R.1    Lenzen, R.2    Sies, H.3
  • 12
    • 0001839405 scopus 로고
    • Functional aspects of glutathione disulfide and hidden forms of glutathione
    • Eds. Arias IM and Jakoby WB, Raven Press, New York
    • 12. Kosower NS and Kosower EM, Functional aspects of glutathione disulfide and hidden forms of glutathione. In: Glutathione Metabolism and Function (Eds. Arias IM and Jakoby WB), pp. 159-174. Raven Press, New York, 1976.
    • (1976) Glutathione Metabolism and Function , pp. 159-174
    • Kosower, N.S.1    Kosower, E.M.2
  • 14
    • 0020624295 scopus 로고
    • Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide
    • 14. Brigelius R, Muckel C, Akerboom TPM and Sies H, Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide. Biochem Pharmacol 32: 2529-2534, 1983.
    • (1983) Biochem Pharmacol , vol.32 , pp. 2529-2534
    • Brigelius, R.1    Muckel, C.2    Akerboom, T.P.M.3    Sies, H.4
  • 15
    • 0023135172 scopus 로고
    • Measurement of tissue sulfhydryls and disulfides in tissue protein and nonprotein fractions by high performance liquid chromatography using electrochemical detection
    • 15. Dupuy D and Szabo S, Measurement of tissue sulfhydryls and disulfides in tissue protein and nonprotein fractions by high performance liquid chromatography using electrochemical detection. J Liq Chromatog 10: 107-119, 1987.
    • (1987) J Liq Chromatog , vol.10 , pp. 107-119
    • Dupuy, D.1    Szabo, S.2
  • 16
    • 0020162308 scopus 로고
    • Reduced, oxidized, and protein-bound glutathione concentrations in normal and cataractous lenses in the dog
    • 16. Gelatt KN, Bruss M, DeCostanza SM, Noonan NE, Das ND and Wolf ED, Reduced, oxidized, and protein-bound glutathione concentrations in normal and cataractous lenses in the dog. Am J Vet Res 43: 1215-1217, 1982.
    • (1982) Am J Vet Res , vol.43 , pp. 1215-1217
    • Gelatt, K.N.1    Bruss, M.2    DeCostanza, S.M.3    Noonan, N.E.4    Das, N.D.5    Wolf, E.D.6
  • 17
    • 0027292791 scopus 로고
    • Effect of oxidant exposure on thiol status in the intestinal mucosa
    • 17. Benard O and Balasubramanian KA, Effect of oxidant exposure on thiol status in the intestinal mucosa. Biochem Pharmacol 45: 2011-2015, 1993.
    • (1993) Biochem Pharmacol , vol.45 , pp. 2011-2015
    • Benard, O.1    Balasubramanian, K.A.2
  • 18
    • 0014248678 scopus 로고
    • Cellular mixed disulfides between thiols and proteins, and their possible implication for radiation protection
    • 18. Modig H, Cellular mixed disulfides between thiols and proteins, and their possible implication for radiation protection. Biochem Pharmacol 17: 177-186, 1968.
    • (1968) Biochem Pharmacol , vol.17 , pp. 177-186
    • Modig, H.1
  • 19
    • 0014787125 scopus 로고
    • Free and bound glutathione in normal and cataractous human lenses
    • 19. Harding JJ, Free and bound glutathione in normal and cataractous human lenses. Biochem J 117: 957-960, 1970.
    • (1970) Biochem J , vol.117 , pp. 957-960
    • Harding, J.J.1
  • 20
    • 0000863301 scopus 로고
    • Protein-bound glutathione in mammalian lenses and in galactose cataract
    • 20. Reddy VN and Han RF, Protein-bound glutathione in mammalian lenses and in galactose cataract. Doc Ophthalmol Proc Series 8: 153-160, 1976.
    • (1976) Doc Ophthalmol Proc Series , vol.8 , pp. 153-160
    • Reddy, V.N.1    Han, R.F.2
  • 21
    • 0026572110 scopus 로고
    • Reversible activation of soluble guanylate cyclase by oxidizing agents
    • 21. Wu XB, Brune B, von Appen F and Ullrich V, Reversible activation of soluble guanylate cyclase by oxidizing agents. Arch Biochem Biophys 294: 75-82, 1992.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 75-82
    • Wu, X.B.1    Brune, B.2    Von Appen, F.3    Ullrich, V.4
  • 22
    • 0027248275 scopus 로고
    • Homocysteine and other thiols determined in plasma by HPLC and thiol-specific postcolumn derivatization
    • 22. Andersson A, Isaksson A, Brattström L and Hultberg B, Homocysteine and other thiols determined in plasma by HPLC and thiol-specific postcolumn derivatization. Clin Chem 39: 1590-1597, 1993.
    • (1993) Clin Chem , vol.39 , pp. 1590-1597
    • Andersson, A.1    Isaksson, A.2    Brattström, L.3    Hultberg, B.4
  • 23
    • 0026515778 scopus 로고
    • Determination of the in vivo redox status of cysteine, cysteinylglycine, homocysteine, and glutathione in human plasma
    • 23. Mansoor MA, Svardal AM and Ueland PM, Determination of the in vivo redox status of cysteine, cysteinylglycine, homocysteine, and glutathione in human plasma. Anal Biochem 200: 218-229, 1992.
    • (1992) Anal Biochem , vol.200 , pp. 218-229
    • Mansoor, M.A.1    Svardal, A.M.2    Ueland, P.M.3
  • 25
    • 0026075333 scopus 로고
    • L-2-Oxothia-zolidine-4-carboxylic acid (OTC), a cysteine prodrug: Pharmacokinetics and effects on thiols in plasma and lymphocytes of man
    • 25. Porta P, Aebi S, Summer K and Lauterberg BH, L-2-Oxothia-zolidine-4-carboxylic acid (OTC), a cysteine prodrug: Pharmacokinetics and effects on thiols in plasma and lymphocytes of man. J Pharmacol Exp Ther 257: 331-334, 1991.
    • (1991) J Pharmacol Exp Ther , vol.257 , pp. 331-334
    • Porta, P.1    Aebi, S.2    Summer, K.3    Lauterberg, B.H.4
  • 26
    • 0025100797 scopus 로고
    • Determination of reduced, oxidized and protein-bound glutathione in human plasma with precolumn derivatization with monobromobimane and liquid chromatography
    • 26. Svardal AM, Mansoor MA and Ueland PM, Determination of reduced, oxidized and protein-bound glutathione in human plasma with precolumn derivatization with monobromobimane and liquid chromatography. Anal Biochem 184: 338-346, 1990.
    • (1990) Anal Biochem , vol.184 , pp. 338-346
    • Svardal, A.M.1    Mansoor, M.A.2    Ueland, P.M.3
  • 27
    • 0023812019 scopus 로고
    • Determination of cysteine, glutathione and N-acetylcysteine in plasma by ion-pair reversed-phase liquid chromatography and post-column derivatization
    • 27. Johansson M and Lenngren S, Determination of cysteine, glutathione and N-acetylcysteine in plasma by ion-pair reversed-phase liquid chromatography and post-column derivatization. J Chromatogr 432: 65-74, 1988.
    • (1988) J Chromatogr , vol.432 , pp. 65-74
    • Johansson, M.1    Lenngren, S.2
  • 28
    • 0022602307 scopus 로고
    • The effect of fasting on leukocyte and plasma glutathione and sulfur amino acid concentrations
    • 28. Märtenssen J, The effect of fasting on leukocyte and plasma glutathione and sulfur amino acid concentrations. Metabolism 35: 118-121, 1986.
    • (1986) Metabolism , vol.35 , pp. 118-121
    • Märtenssen, J.1
  • 29
    • 0027462812 scopus 로고
    • Homocysteine and other thiols in plasma and urine: Automated determination and sample stability
    • 29. Fiskerstrand T, Refsum H, Kvalheim G and Ueland PM, Homocysteine and other thiols in plasma and urine: Automated determination and sample stability. Clin Chem 39: 263-271, 1993.
    • (1993) Clin Chem , vol.39 , pp. 263-271
    • Fiskerstrand, T.1    Refsum, H.2    Kvalheim, G.3    Ueland, P.M.4
  • 30
    • 0024465521 scopus 로고
    • Plasma sulfhydryl-containing amino acids in patients with cerebral infarction and in hypertensive subjects
    • 30. Araki A, Sako Y, Fukushima Y, Matsumoto M, Asada T and Kita T, Plasma sulfhydryl-containing amino acids in patients with cerebral infarction and in hypertensive subjects. Atherosclerosis 79: 139-146, 1989.
    • (1989) Atherosclerosis , vol.79 , pp. 139-146
    • Araki, A.1    Sako, Y.2    Fukushima, Y.3    Matsumoto, M.4    Asada, T.5    Kita, T.6
  • 31
    • 0023845397 scopus 로고
    • Interrelations between plasma free and protein-bound homocysteine in homocystinuria
    • 31. Wiley VC, Dudman NPB and Wilcken DEL, Interrelations between plasma free and protein-bound homocysteine in homocystinuria. Metabolism 37: 191-195, 1988.
    • (1988) Metabolism , vol.37 , pp. 191-195
    • Wiley, V.C.1    Dudman, N.P.B.2    Wilcken, D.E.L.3
  • 32
    • 0023269373 scopus 로고
    • Altered plasma free and protein-bound sulfur amino acid levels in patients undergoing maintenance hemodialysis
    • 32. Smolin LN, Laidlaw SA and Kopple JD, Altered plasma free and protein-bound sulfur amino acid levels in patients undergoing maintenance hemodialysis. Am J Clin Nutr 45: 737-743, 1987.
    • (1987) Am J Clin Nutr , vol.45 , pp. 737-743
    • Smolin, L.N.1    Laidlaw, S.A.2    Kopple, J.D.3
  • 34
    • 0019854760 scopus 로고
    • A method for measurement of free and bound plasma cyst(e)ine
    • 34. Malloy MH, Rassin DK and Gaull GE, A method for measurement of free and bound plasma cyst(e)ine. Anal Biochem 113: 407-415, 1981.
    • (1981) Anal Biochem , vol.113 , pp. 407-415
    • Malloy, M.H.1    Rassin, D.K.2    Gaull, G.E.3
  • 35
    • 0002516623 scopus 로고
    • Routine hematology procedure
    • Chap. 3, Lea & Febiger, Philadelphia
    • 35. Brown BA, Routine hematology procedure. In: Hematology: Principles and Procedures, 6th Edn, Chap. 3, pp. 83-102. Lea & Febiger, Philadelphia, 1993.
    • (1993) Hematology: Principles and Procedures, 6th Edn , pp. 83-102
    • Brown, B.A.1
  • 37
    • 0017804230 scopus 로고
    • Glutathione and γ-glutamylcysteine in whole blood, plasma and erythrocytes
    • 37. Hagenfeldt L, Arvidsson A and Larsson A, Glutathione and γ-glutamylcysteine in whole blood, plasma and erythrocytes. Clin Chim Acta 85: 167-173, 1978.
    • (1978) Clin Chim Acta , vol.85 , pp. 167-173
    • Hagenfeldt, L.1    Arvidsson, A.2    Larsson, A.3
  • 38
    • 0014124577 scopus 로고
    • Disulfide and sulfhydryl compounds in TCA extracts of human blood and plasma
    • 38. Ellman GL and Lysko H, Disulfide and sulfhydryl compounds in TCA extracts of human blood and plasma. J Lab Clin Med 70: 518-527, 1967.
    • (1967) J Lab Clin Med , vol.70 , pp. 518-527
    • Ellman, G.L.1    Lysko, H.2
  • 39
    • 0012018546 scopus 로고
    • The distribution of free amino acids between erythrocytes and plasma in man
    • 39. Johnson CA and Bergeim O, The distribution of free amino acids between erythrocytes and plasma in man. J Biol Chem 188: 833-838, 1951.
    • (1951) J Biol Chem , vol.188 , pp. 833-838
    • Johnson, C.A.1    Bergeim, O.2
  • 40
    • 0015137746 scopus 로고
    • Comparison of amino acid concentrations between plasma and erythrocytes. Studies in normal human subjects and those with metabolic disorders
    • 40. Levy HL and Barkin E, Comparison of amino acid concentrations between plasma and erythrocytes. Studies in normal human subjects and those with metabolic disorders. J Lab Clin Med 78: 517-523, 1971.
    • (1971) J Lab Clin Med , vol.78 , pp. 517-523
    • Levy, H.L.1    Barkin, E.2
  • 41
    • 0019777335 scopus 로고
    • Analysis of biological thiols: Derivatization with monobromobimane and separation by reverse-phase high-performance liquid chromatography
    • 41. Newton GL, Dorian R and Fahey RC, Analysis of biological thiols: Derivatization with monobromobimane and separation by reverse-phase high-performance liquid chromatography. Anal Biochem 114: 383-387, 1981.
    • (1981) Anal Biochem , vol.114 , pp. 383-387
    • Newton, G.L.1    Dorian, R.2    Fahey, R.C.3
  • 42
    • 0018865969 scopus 로고
    • The distribution of amino acids between plasma and erythrocytes
    • 42. Hagenfeldt L and Arvidsson A, The distribution of amino acids between plasma and erythrocytes. Clin Chim Acta 100: 133-141, 1980.
    • (1980) Clin Chim Acta , vol.100 , pp. 133-141
    • Hagenfeldt, L.1    Arvidsson, A.2
  • 43
    • 0025372079 scopus 로고
    • The effects of changes in plasma amino acid concentrations on erythrocyte amino acid content
    • 43. Schaefer A, Piquard F and Haberey P, The effects of changes in plasma amino acid concentrations on erythrocyte amino acid content. Clin Biochem 23: 237-240, 1990.
    • (1990) Clin Biochem , vol.23 , pp. 237-240
    • Schaefer, A.1    Piquard, F.2    Haberey, P.3
  • 44
    • 0018600786 scopus 로고
    • Formation of disulfide bonds between glutathione and membrane SH groups in human erythrocytes
    • 44. Haest CWM, Kamp D and Deuticke B, Formation of disulfide bonds between glutathione and membrane SH groups in human erythrocytes. Biochim Biophys Acta 557: 363-371, 1979.
    • (1979) Biochim Biophys Acta , vol.557 , pp. 363-371
    • Haest, C.W.M.1    Kamp, D.2    Deuticke, B.3
  • 45
    • 0001234513 scopus 로고
    • The sulfur chemistry of proteins
    • Eds. Anfinsen CB, Anson ML, Bailey K and Edsell JT, Academic Press, New York
    • 45. Cecil R and McPhee JR, The sulfur chemistry of proteins. In: Advances in Protein Chemistry (Eds. Anfinsen CB, Anson ML, Bailey K and Edsell JT), Vol. XIV, pp. 255-389. Academic Press, New York, 1959.
    • (1959) Advances in Protein Chemistry , vol.14 , pp. 255-389
    • Cecil, R.1    McPhee, J.R.2
  • 46
    • 0001439977 scopus 로고
    • Oxidative hemolysis and precipitation of hemoglobin. II. Role of thiols in oxidant drug action
    • 46. Allen DW and Jandl JH, Oxidative hemolysis and precipitation of hemoglobin. II. Role of thiols in oxidant drug action. J Clin Invest 40: 454-475, 1961.
    • (1961) J Clin Invest , vol.40 , pp. 454-475
    • Allen, D.W.1    Jandl, J.H.2
  • 47
    • 0000545193 scopus 로고
    • Studies on the heterogeneity of hemoglobin. V. The binding of hemoglobin with oxidized glutathione
    • 47. Huisman THJ and Dozy AM, Studies on the heterogeneity of hemoglobin. V. The binding of hemoglobin with oxidized glutathione. J Lab Clin Med 60: 302-309, 1962.
    • (1962) J Lab Clin Med , vol.60 , pp. 302-309
    • Huisman, T.H.J.1    Dozy, A.M.2
  • 48
    • 0022828370 scopus 로고
    • Galacteros F and Beuzard Y, Covalent binding of glutathione to hemoglobin
    • 48. Garel M-C, Domenget C, Caburi-Martin J, Prehu C, Galacteros F and Beuzard Y, Covalent binding of glutathione to hemoglobin. J Biol Chem 261: 14704-14709, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 14704-14709
    • Garel, M.-C.1    Domenget, C.2    Caburi-Martin, J.3    Prehu, C.4
  • 49
    • 0014842393 scopus 로고
    • Glutathione metabolism of the erythrocyte. The enzymic cleavage of glutathione-hemoglobin preparations by glutathione reductase
    • 49. Srivastava SK and Beutler E, Glutathione metabolism of the erythrocyte. The enzymic cleavage of glutathione-hemoglobin preparations by glutathione reductase. Biochem J 119: 353-357, 1970.
    • (1970) Biochem J , vol.119 , pp. 353-357
    • Srivastava, S.K.1    Beutler, E.2
  • 50
    • 0019173673 scopus 로고
    • Dynamic state of glutathione in blood plasma
    • 50. Anderson ME and Meister A, Dynamic state of glutathione in blood plasma. J Biol Chem 255: 9530-9533, 1980.
    • (1980) J Biol Chem , vol.255 , pp. 9530-9533
    • Anderson, M.E.1    Meister, A.2
  • 51
    • 0019125693 scopus 로고
    • The level and half-life of glutathione in human plasma
    • 51. Wendel A and Cikryt P, The level and half-life of glutathione in human plasma. FEBS Lett 120: 209-211, 1980.
    • (1980) FEBS Lett , vol.120 , pp. 209-211
    • Wendel, A.1    Cikryt, P.2
  • 52
    • 0021819571 scopus 로고
    • Plasma glutathione in health and in patients with malignant diseases
    • 52. Beutler E and Gelbart T, Plasma glutathione in health and in patients with malignant diseases. J Lab Clin Med 105: 581-584, 1985.
    • (1985) J Lab Clin Med , vol.105 , pp. 581-584
    • Beutler, E.1    Gelbart, T.2
  • 53
    • 0022257875 scopus 로고
    • Distribution of oxidized and reduced forms of glutathione and cysteine in rat plasma
    • 53. Lash HL and Jones DP, Distribution of oxidized and reduced forms of glutathione and cysteine in rat plasma. Arch Biochem Biophys 240: 583-592, 1985.
    • (1985) Arch Biochem Biophys , vol.240 , pp. 583-592
    • Lash, H.L.1    Jones, D.P.2
  • 54
    • 0023630299 scopus 로고
    • Improved procedure for determining glutathione in plasma as an index of myocardial oxidative stress
    • 54. Curello S, Improved procedure for determining glutathione in plasma as an index of myocardial oxidative stress. Clin Chem 33: 1448-1449, 1987.
    • (1987) Clin Chem , vol.33 , pp. 1448-1449
    • Curello, S.1
  • 55
    • 0028921840 scopus 로고
    • Effect of thiol oxidation and thiol export from erythrocytes on determination of redox status of homocysteine and other thiols in plasma from healthy subjects and patients with cerebral infarction
    • 55. Andersson A, Lindren A and Hultberg B, Effect of thiol oxidation and thiol export from erythrocytes on determination of redox status of homocysteine and other thiols in plasma from healthy subjects and patients with cerebral infarction. Clin Chem 41: 361-366, 1995.
    • (1995) Clin Chem , vol.41 , pp. 361-366
    • Andersson, A.1    Lindren, A.2    Hultberg, B.3
  • 57
    • 0000662412 scopus 로고
    • Methionine, homocyst(e)ine, cyst(e)ine - Metabolic relationships
    • Ed. Friedman M, Chap. 8, CRC Press, Boca Raton, FL
    • 57. Smolin LA and Benevenga NJ, Methionine, homocyst(e)ine, cyst(e)ine - Metabolic relationships. In: Absorption and Utilization of Amino Acids (Ed. Friedman M), Vol. I, Chap. 8, pp. 157-187. CRC Press, Boca Raton, FL, 1989.
    • (1989) Absorption and Utilization of Amino Acids , vol.1 , pp. 157-187
    • Smolin, L.A.1    Benevenga, N.J.2
  • 59
    • 0028901371 scopus 로고
    • Redox status and protein binding of plasma homocysteine and other aminothiols in patients with early-onset peripheral vascular disease
    • 59. Mansoor MA, Bergmark C, Svardal MA, Lonning PE and Ueland PM, Redox status and protein binding of plasma homocysteine and other aminothiols in patients with early-onset peripheral vascular disease. Arterioscler Thromb Vasc Biol 15: 232-240, 1995.
    • (1995) Arterioscler Thromb Vasc Biol , vol.15 , pp. 232-240
    • Mansoor, M.A.1    Bergmark, C.2    Svardal, M.A.3    Lonning, P.E.4    Ueland, P.M.5
  • 60
    • 0028088018 scopus 로고
    • Plasma homocysteine and thiol compound fractions after oral administration of N-acetylcysteine
    • 60. Hultberg B, Andersson A, Masson P, Larson M and Tunek A, Plasma homocysteine and thiol compound fractions after oral administration of N-acetylcysteine. Scand J Clin Lab Invest 54: 417-422, 1994.
    • (1994) Scand J Clin Lab Invest , vol.54 , pp. 417-422
    • Hultberg, B.1    Andersson, A.2    Masson, P.3    Larson, M.4    Tunek, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.