메뉴 건너뛰기




Volumn 129, Issue 5, 1991, Pages 2647-2654

Cyclosporin-mediated depression of luteinizing hormone receptors and heme biosynthesis in rat testes: A possible mechanism for decrease in serum testosterone

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOSPORIN A; FOLLITROPIN; HEME; LUTEINIZING HORMONE; LUTEINIZING HORMONE RECEPTOR; TESTOSTERONE;

EID: 0025838784     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/endo-129-5-2647     Document Type: Article
Times cited : (33)

References (59)
  • 1
    • 0024947768 scopus 로고
    • Pathophysiology and toxicology of cyclosporin in humans and animals
    • Mason J 1989 Pathophysiology and toxicology of cyclosporin in humans and animals. Pharmacol Rev 41:423-434
    • (1989) Pharmacol Rev , vol.41 , pp. 423-434
    • Mason, J.1
  • 2
    • 0025285505 scopus 로고
    • Renal side-effects of cyclosporin
    • Mason J 1990 Renal side-effects of cyclosporin. Transplant Proc 22:1280-1283
    • (1990) Transplant Proc , vol.22 , pp. 1280-1283
    • Mason, J.1
  • 3
    • 0039897482 scopus 로고
    • Cyclosporine A and hypertension
    • Schachter M 1988 Cyclosporine A and hypertension. J Hypertension 6:511-516
    • (1988) J Hypertension , vol.6 , pp. 511-516
    • Schachter, M.1
  • 5
    • 0023215854 scopus 로고
    • Cyclosporin inhibits testosterone biosynthesis in the rat testis
    • Rajfer J, Sikka SC, Lemmi C, Koyle MA 1987 Cyclosporin inhibits testosterone biosynthesis in the rat testis. Endocrinology 121:586-589
    • (1987) Endocrinology , vol.121 , pp. 586-589
    • Rajfer, J.1    Sikka, S.C.2    Lemmi, C.3    Koyle, M.A.4
  • 7
    • 0025012846 scopus 로고
    • Evaluation of the effect of experimental cyclosporine toxicity on male reproduction and renal function
    • Seethalakshmi L, Flores C, Khauli RB, Diamond DA, Menon M 1990 Evaluation of the effect of experimental cyclosporine toxicity on male reproduction and renal function. Transplantation 49:17-19
    • (1990) Transplantation , vol.49 , pp. 17-19
    • Seethalakshmi, L.1    Flores, C.2    Khauli, R.B.3    Diamond, D.A.4    Menon, M.5
  • 8
    • 0023740255 scopus 로고
    • Effects of cyclosporine on the hypothalamic-pituitary-gonadal axis in the male rat: Mechanism of action
    • Sikka SC, Bhasin S, Coy DC, Koyle MA, Swerdloff RS, Rajfer J 1988 Effects of cyclosporine on the hypothalamic-pituitary-gonadal axis in the male rat: Mechanism of action. Endocrinology 123:1069-1074
    • (1988) Endocrinology , vol.123 , pp. 1069-1074
    • Sikka, S.C.1    Bhasin, S.2    Coy, D.C.3    Koyle, M.A.4    Swerdloff, R.S.5    Rajfer, J.6
  • 9
    • 0024232229 scopus 로고
    • Effect of cyclosporin on steroidogenesis in rat Leydig cells
    • Sikka SC, Coy DC, Lemmi CAE, Rajfer J 1988 Effect of cyclosporin on steroidogenesis in rat Leydig cells. Transplantation 46:886-889
    • (1988) Transplantation , vol.46 , pp. 886-889
    • Sikka, S.C.1    Coy, D.C.2    Lemmi, C.3    Rajfer, J.4
  • 11
    • 0023895692 scopus 로고
    • Cyclosporin-induced testicular dysfunction: A separation of the nephrotoxic component and an assessment of a 60-day recovery period
    • Seethalakshmi L, Diamond DA, Malhotra RK, Mazanitis SC, Kumar S, Menon M 1988 Cyclosporin-induced testicular dysfunction: A separation of the nephrotoxic component and an assessment of a 60-day recovery period. Transplant Proc 20:1005-1010
    • (1988) Transplant Proc , vol.20 , pp. 1005-1010
    • Seethalakshmi, L.1    Diamond, D.A.2    Malhotra, R.K.3    Mazanitis, S.C.4    Kumar, S.5    Menon, M.6
  • 13
    • 0018764719 scopus 로고
    • Hormonal regulation of peptide receptors and target cell responses
    • Catt KJ, Harwood JP, Aguilera G, Dufau ML 1979 Hormonal regulation of peptide receptors and target cell responses. Nature 280:109-116
    • (1979) Nature , vol.280 , pp. 109-116
    • Catt, K.J.1    Harwood, J.P.2    Aguilera, G.3    Dufau, M.L.4
  • 14
    • 0017850766 scopus 로고
    • Regulation of luteinizing hormone receptors and steroidogenesis in gonadotropin-desensi-tized Leydig cells
    • Cigorraga S, Dufau ML, Catt KJ 1978 Regulation of luteinizing hormone receptors and steroidogenesis in gonadotropin-desensi-tized Leydig cells. J Biol Chem 253:4297-4304
    • (1978) J Biol Chem , vol.253 , pp. 4297-4304
    • Cigorraga, S.1    Dufau, M.L.2    Catt, K.J.3
  • 15
    • 0019844590 scopus 로고
    • Modulation of Leydig cell androgen biosynthesis and cytochrome P-450 levels during estrogen treatment and human chorionic gonadotropin-induced desensitization
    • Nozu R, Matsuura S, Catt KJ, Dufau ML 1981 Modulation of Leydig cell androgen biosynthesis and cytochrome P-450 levels during estrogen treatment and human chorionic gonadotropin-induced desensitization. J Biol Chem 256:10012-10016
    • (1981) J Biol Chem , vol.256 , pp. 10012-10016
    • Nozu, R.1    Matsuura, S.2    Catt, K.J.3    Dufau, M.L.4
  • 16
    • 0025214553 scopus 로고
    • Hormonal regulation of cytochrome P450 enzymes, cholesterol side chain cleavage and 17 alpha hydroxylase/C 17-20 lyase in Leydig cells
    • Payne AH 1990 Hormonal regulation of cytochrome P450 enzymes, cholesterol side chain cleavage and 17 alpha hydroxylase/C 17-20 lyase in Leydig cells. Biol Reprod 42:399-404
    • (1990) Biol Reprod , vol.42 , pp. 399-404
    • Payne, A.H.1
  • 17
    • 0022770127 scopus 로고
    • Cytochromes P-450 and the regulation of steroid synthesis
    • Hall PF 1986 Cytochromes P-450 and the regulation of steroid synthesis. Steroids 48:131-196
    • (1986) Steroids , vol.48 , pp. 131-196
    • Hall, P.F.1
  • 18
    • 0025340851 scopus 로고
    • Cis-platinum-mediated depression of LH receptors and cytochrome P-450scc in rat Leydig cells: A possible mechanism for decrease in serum testosterone
    • Maines MD, Sluss PM, Iscan M 1990 Cis-platinum-mediated depression of LH receptors and cytochrome P-450scc in rat Leydig cells: A possible mechanism for decrease in serum testosterone. Endocrinology 126:2398-2406
    • (1990) Endocrinology , vol.126 , pp. 2398-2406
    • Maines, M.D.1    Sluss, P.M.2    Iscan, M.3
  • 19
    • 0025172766 scopus 로고
    • Effect of cis-platinum on heme, drug and steroid metabolism pathways: Possible involvement in infertility and nephrotoxicity
    • Maines MD 1990 Effect of cis-platinum on heme, drug and steroid metabolism pathways: Possible involvement in infertility and nephrotoxicity. CRC Crit Rev Toxicol 21:1-20
    • (1990) CRC Crit Rev Toxicol , vol.21 , pp. 1-20
    • Maines, M.D.1
  • 20
    • 0019887951 scopus 로고
    • Microsomal cytochrome P-450 from neonatal pig testis
    • Nakajin S, Hall PF 1981 Microsomal cytochrome P-450 from neonatal pig testis. J Biol Chem 256:3871-3876
    • (1981) J Biol Chem , vol.256 , pp. 3871-3876
    • Nakajin, S.1    Hall, P.F.2
  • 21
    • 0021289258 scopus 로고
    • C21 steroid side chain cleavage enzyme from porcine adrenal micro-somes
    • Nakajin S, Shinoda M, Haniu M, Shively JE, Hall PF 1984 C21 steroid side chain cleavage enzyme from porcine adrenal micro-somes. J Biol Chem 259:3971-3976
    • (1984) J Biol Chem , vol.259 , pp. 3971-3976
    • Nakajin, S.1    Shinoda, M.2    Haniu, M.3    Shively, J.E.4    Hall, P.F.5
  • 22
    • 0023683485 scopus 로고
    • Combined 17α-hydroxylase/17, 20-lyase deficiency due to a stop codon in the N-terminal region of 17α-hydroxylase cytochrome P-450
    • Yanase T, Kagimoto M, Matsui N, Simpson ER, Waterman MR 1988 Combined 17α-hydroxylase/17, 20-lyase deficiency due to a stop codon in the N-terminal region of 17α-hydroxylase cytochrome P-450. Mol Cell Endocrinol 59:249-253
    • (1988) Mol Cell Endocrinol , vol.59 , pp. 249-253
    • Yanase, T.1    Kagimoto, M.2    Matsui, N.3    Simpson, E.R.4    Waterman, M.R.5
  • 23
    • 0022847113 scopus 로고
    • Expression of bovine 17α-hydroxylase cytochrome P-450 cDNA in nonsteroidogenic (COS 1) cells
    • Zuber MX, Simpson ER, Waterman MR 1986 Expression of bovine 17α-hydroxylase cytochrome P-450 cDNA in nonsteroidogenic (COS 1) cells. Science 234:1258-1261
    • (1986) Science , vol.234 , pp. 1258-1261
    • Zuber, M.X.1    Simpson, E.R.2    Waterman, M.R.3
  • 24
    • 0020406031 scopus 로고
    • Inhibition of testicular heme oxygenase activity by cadmium: A novel cellular response
    • Maines MD, Chung AS, Kutty RK 1982 Inhibition of testicular heme oxygenase activity by cadmium: A novel cellular response. J Biol Chem 257:14116-14121
    • (1982) J Biol Chem , vol.257 , pp. 14116-14121
    • Maines, M.D.1    Chung, A.S.2    Kutty, R.K.3
  • 25
    • 0014027226 scopus 로고
    • The induction in vitro of the synthesis of δ-aminolevulinic acid synthetase in chemical porphyria: A response to certain drugs, sex hormones, and foreign chemicals
    • Granick S 1966 The induction in vitro of the synthesis of δ-aminolevulinic acid synthetase in chemical porphyria: A response to certain drugs, sex hormones, and foreign chemicals. J Biol Chem 241:1359-1375
    • (1966) J Biol Chem , vol.241 , pp. 1359-1375
    • Granick, S.1
  • 26
    • 0024587598 scopus 로고
    • Differential effects of cyclosporin on hepatic and renal heme, cytochrome P-450 and drug metabolism: Possible role in nephrotoxicity of the drug
    • Mayer RD, Berman S, Cockett ATK, Maines MD 1989 Differential effects of cyclosporin on hepatic and renal heme, cytochrome P-450 and drug metabolism: Possible role in nephrotoxicity of the drug. Biochem Pharmacol 38:1001-1007
    • (1989) Biochem Pharmacol , vol.38 , pp. 1001-1007
    • Mayer, R.D.1    Berman, S.2    Cockett, A.3    Maines, M.D.4
  • 28
    • 0021141190 scopus 로고
    • Dissociation of heme metabolic activities from the microsomal cytochrome P-450 turnover in testis of hypophysectomized rats
    • Maines MD, Jollie DR 1984 Dissociation of heme metabolic activities from the microsomal cytochrome P-450 turnover in testis of hypophysectomized rats. J Biol Chem 259:9557-9562
    • (1984) J Biol Chem , vol.259 , pp. 9557-9562
    • Maines, M.D.1    Jollie, D.R.2
  • 29
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T, Sato R 1964 The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239:2370-2378
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 30
    • 0000756628 scopus 로고
    • The molar light absorption of pyridine ferroprotoporphyrin
    • Paul KC, Theorell H, Akeson A 1953 The molar light absorption of pyridine ferroprotoporphyrin. Acta Chem Scand 7:1284-1287
    • (1953) Acta Chem Scand , vol.7 , pp. 1284-1287
    • Paul, K.C.1    Theorell, H.2    Akeson, A.3
  • 31
    • 0016768918 scopus 로고
    • Effects by heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium, and a spectrofluorometric assay for porphyrin composition
    • Granick S, Sinclair P, Sassa S, Grieninger G 1975 Effects by heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium, and a spectrofluorometric assay for porphyrin composition. J Biol Chem 250:9215-9225
    • (1975) J Biol Chem , vol.250 , pp. 9215-9225
    • Granick, S.1    Sinclair, P.2    Sassa, S.3    Grieninger, G.4
  • 32
    • 0021798616 scopus 로고
    • Inhibition of testicular cytochrome P-450 dependent steroid biosynthesis by cis-platinum
    • Maines MD, Mayer RD 1985 Inhibition of testicular cytochrome P-450 dependent steroid biosynthesis by cis-platinum. J Biol Chem 260:6063-6068
    • (1985) J Biol Chem , vol.260 , pp. 6063-6068
    • Maines, M.D.1    Mayer, R.D.2
  • 33
    • 0015858864 scopus 로고
    • A modified method for the assay of benzo(A)pyrene hydroxylase
    • Dehnen W, Tomingas R, Roos J 1973 A modified method for the assay of benzo(a)pyrene hydroxylase. Anal Biochem 53:373-383
    • (1973) Anal Biochem , vol.53 , pp. 373-383
    • Dehnen, W.1    Tomingas, R.2    Roos, J.3
  • 34
    • 0023029882 scopus 로고
    • Cadmium-mediated inhibition of testicular heme oxygenase activity: The role of NADPH-cytochrome c (P-450) reductase
    • Trakshel GM, Kutty RK, Maines MD 1986 Cadmium-mediated inhibition of testicular heme oxygenase activity: The role of NADPH-cytochrome c (P-450) reductase. Arch Biochem Biophys 251:175-187
    • (1986) Arch Biochem Biophys , vol.251 , pp. 175-187
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 35
    • 0006476631 scopus 로고
    • Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity
    • Maines MD, Kappas A 1974 Cobalt induction of hepatic heme oxygenase; with evidence that cytochrome P-450 is not essential for this enzyme activity. Proc Natl Acad Sci USA 71:4293-4297
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 4293-4297
    • Maines, M.D.1    Kappas, A.2
  • 36
    • 0017795019 scopus 로고
    • Purification and properties of NADPH-cytochrome P-450 reductase
    • Fleischer S, Packer L (eds), Academic Press, New York
    • Strobel HW, Dignam JD 1978 Purification and properties of NADPH-cytochrome P-450 reductase. In: Fleischer S, Packer L (eds) Methods in Enzymology. Academic Press, New York, vol 52:89-96
    • (1978) Methods in Enzymology , vol.52 , pp. 89-96
    • Strobel, H.W.1    Dignam, J.D.2
  • 37
    • 0018171369 scopus 로고
    • Control of steroid metabolism in rat adrenal mitochondria
    • Mason JI, Arthur JR, Boyd GS 1978 Control of steroid metabolism in rat adrenal mitochondria. Biochem J 174:1045-1051
    • (1978) Biochem J , vol.174 , pp. 1045-1051
    • Mason, J.I.1    Arthur, J.R.2    Boyd, G.S.3
  • 38
    • 0022908021 scopus 로고
    • Alterations of heme, cytochrome P-450, and steroid metabolism by mercury in rat adrenals
    • Veltman JC, Maines MD 1986 Alterations of heme, cytochrome P-450, and steroid metabolism by mercury in rat adrenals. Arch Biochem Biophys 248:467-478
    • (1986) Arch Biochem Biophys , vol.248 , pp. 467-478
    • Veltman, J.C.1    Maines, M.D.2
  • 40
    • 0019209805 scopus 로고
    • Regional distribution of the enzymes of haem biosynthesis and the inhibition of δ-aminolevulinate synthetase by manganese in the rat brain
    • Maines MD 1980 Regional distribution of the enzymes of haem biosynthesis and the inhibition of δ-aminolevulinate synthetase by manganese in the rat brain. Biochem J 190:315-321
    • (1980) Biochem J , vol.190 , pp. 315-321
    • Maines, M.D.1
  • 41
    • 78651057641 scopus 로고
    • The occurance and determination of δ-aminolevulinic acid and porphobilinogen in urine
    • Mauzerall D, Granick S 1956 The occurance and determination of δ-aminolevulinic acid and porphobilinogen in urine. J Biol Chem 219:435-466
    • (1956) J Biol Chem , vol.219 , pp. 435-466
    • Mauzerall, D.1    Granick, S.2
  • 42
    • 0015400141 scopus 로고
    • Assays for porphyrins, δ-aminolevulinc-acid dehydratase, and porphyri-nogen synthetase in microliter samples of blood: Applications to metabolic defects involving the heme pathway
    • Granick S, Sassa S, Granick JL, Lever RD, Kappas A 1972 Assays for porphyrins, δ-aminolevulinc-acid dehydratase, and porphyri-nogen synthetase in microliter samples of blood: Applications to metabolic defects involving the heme pathway. Proc Natl Acad Sci USA 69:2381-2385
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 2381-2385
    • Granick, S.1    Sassa, S.2    Granick, J.L.3    Lever, R.D.4    Kappas, A.5
  • 43
    • 0014545574 scopus 로고
    • The structural organization of haem synthesis in rat liver mitochondria
    • Jones MS, Jones OTG 1969 The structural organization of haem synthesis in rat liver mitochondria. Biochem J 113:507-514
    • (1969) Biochem J , vol.113 , pp. 507-514
    • Jones, M.S.1    Jones, O.2
  • 45
    • 0019132846 scopus 로고
    • Hormone-induced guanyl nucleotide binding and activation of adenylate cyclase in the Leydig cell
    • Dufau ML, Baukal AJ, Catt KJ 1980 Hormone-induced guanyl nucleotide binding and activation of adenylate cyclase in the Leydig cell. Proc Natl Acad Sci USA 77:5837-5841
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5837-5841
    • Dufau, M.L.1    Baukal, A.J.2    Catt, K.J.3
  • 46
    • 0023061373 scopus 로고
    • P-450 genes: Structure, evolution, and regulation
    • Nebert DW, Gonzalez FJ 1987 P-450 genes: Structure, evolution, and regulation. Annu Rev Biochem 56:945-993
    • (1987) Annu Rev Biochem , vol.56 , pp. 945-993
    • Nebert, D.W.1    Gonzalez, F.J.2
  • 47
    • 0001571980 scopus 로고
    • δ-Aminolevulinic acid, its role in the biosynthesis of porphyrines and purines
    • Shemin D, Russell CS 1953 δ-Aminolevulinic acid, its role in the biosynthesis of porphyrines and purines. J Am Chem Soc 75:4873-4874
    • (1953) J am Chem Soc , vol.75 , pp. 4873-4874
    • Shemin, D.1    Russell, C.S.2
  • 48
    • 34548143967 scopus 로고
    • Aminolaevulinic acid and porphyrin synthesis
    • Neuberger A, Scott JJ 1953 Aminolaevulinic acid and porphyrin synthesis. Nature 172:1093-1094
    • (1953) Nature , vol.172 , pp. 1093-1094
    • Neuberger, A.1    Scott, J.J.2
  • 49
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines MD 1988 Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J 2:2557-2568
    • (1988) FASEB J , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 50
    • 0019888755 scopus 로고
    • Rat liver ferrochelatase purification, properties, and stimulation by fatty acids
    • Taketani S, Tokunaga R 1981 Rat liver ferrochelatase purification, properties, and stimulation by fatty acids. J Biol Chem 256:12748-12753
    • (1981) J Biol Chem , vol.256 , pp. 12748-12753
    • Taketani, S.1    Tokunaga, R.2
  • 51
    • 0024346860 scopus 로고
    • New proposal for the mechanism of cyclosporine A nephrotoxicity: Inhibition of renal microsomal protein chain elongation following in vivo cyclosporine A
    • Buss WC, Stepanek J, Bennett WM 1989 New proposal for the mechanism of cyclosporine A nephrotoxicity: Inhibition of renal microsomal protein chain elongation following in vivo cyclosporine A. Biochem Pharmacol 38:4085-4093
    • (1989) Biochem Pharmacol , vol.38 , pp. 4085-4093
    • Buss, W.C.1    Stepanek, J.2    Bennett, W.M.3
  • 52
    • 0024953181 scopus 로고
    • Pharmacology of cyclosporine. VI. Cellular activation: Regulation of intracellular events by cyclosporine
    • Ryffel B 1989 Pharmacology of cyclosporine. VI. Cellular activation: Regulation of intracellular events by cyclosporine. Pharmacol Rev 41:407-422
    • (1989) Pharmacol Rev , vol.41 , pp. 407-422
    • Ryffel, B.1
  • 53
    • 0023818368 scopus 로고
    • 19F nuclear magnetic resonance studies of cyclosporine and model unilamellar vesicles: Where does the drug sit within the membrane?
    • Rossaro L, Dowd SR, Ho C, Van Theil DH 1988 19F nuclear magnetic resonance studies of cyclosporine and model unilamellar vesicles: Where does the drug sit within the membrane? Transplant Proc 20:41-45
    • (1988) Transplant Proc , vol.20 , pp. 41-45
    • Rossaro, L.1    Dowd, S.R.2    Ho, C.3    Van Theil, D.H.4
  • 54
    • 0015935510 scopus 로고
    • Characterization of an adrenal activator for cholesterol side chain cleavage
    • Kan KW, Ungar F 1973 Characterization of an adrenal activator for cholesterol side chain cleavage. J Biol Chem 248:2868-2875
    • (1973) J Biol Chem , vol.248 , pp. 2868-2875
    • Kan, K.W.1    Ungar, F.2
  • 55
    • 0018142932 scopus 로고
    • Effects of adrenal steroid activator protein on the conversion of various 20 and 22 hydroxy-cholesterols to pregnenolone by adrenal mitochondrial enzymes
    • Teicher BA, Shikita M, Talalay P 1978 Effects of adrenal steroid activator protein on the conversion of various 20 and 22 hydroxy-cholesterols to pregnenolone by adrenal mitochondrial enzymes. Biochem Biophys Res Commun 83:1436-1441
    • (1978) Biochem Biophys Res Commun , vol.83 , pp. 1436-1441
    • Teicher, B.A.1    Shikita, M.2    Talalay, P.3
  • 56
    • 84911691449 scopus 로고
    • Metabolism of free and esterified cholesterol by Leydig cell tumor mitochondria
    • Moyle WR, Jungas RL, Greep RO 1973 Metabolism of free and esterified cholesterol by Leydig cell tumor mitochondria. Biochem J 134:415-424
    • (1973) Biochem J , vol.134 , pp. 415-424
    • Moyle, W.R.1    Jungas, R.L.2    Greep, R.O.3
  • 57
    • 0021248463 scopus 로고
    • Characterization of heme oxygenase in Leydig and Sertoli cells of the rat testes
    • Maines MD 1984 Characterization of heme oxygenase in Leydig and Sertoli cells of the rat testes. Biochem Pharmacol 33:1493-1502
    • (1984) Biochem Pharmacol , vol.33 , pp. 1493-1502
    • Maines, M.D.1
  • 59
    • 0009462074 scopus 로고
    • Historical introduction to porphyrins and porphyries
    • Dailey HA, McGraw-Hill, New York
    • Moore MR 1990 Historical introduction to porphyrins and porphyries. In: Dailey HA (ed) Biosynthesis of Heme and Chlorophylls. McGraw-Hill, New York, pp 1-54
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 1-54
    • Moore, M.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.