메뉴 건너뛰기




Volumn 61, Issue 3, 1996, Pages 126-132

Preparation of an activity-inhibiting monoclonal antibody against human placental aromatase cytochrome P450

Author keywords

aromatase; cytochrome P450; estrogen biosynthesis; monoclonal antibody

Indexed keywords

AROMATASE; AROMATASE INHIBITOR; CYTOCHROME P450; MONOCLONAL ANTIBODY;

EID: 0029916610     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0039-128X(95)00215-C     Document Type: Article
Times cited : (15)

References (25)
  • 1
    • 0016272566 scopus 로고
    • The involvement of human placental microsomal cytochrome P-450 in aromatization
    • Thompson E, Siiteri PK (1974). The involvement of human placental microsomal cytochrome P-450 in aromatization. J Biol Chem 249:5373-5378.
    • (1974) J Biol Chem , vol.249 , pp. 5373-5378
    • Thompson, E.1    Siiteri, P.K.2
  • 2
    • 4243595833 scopus 로고
    • Anti-human placental aromatase II cytochrome P-450 antibody and immunochemical study of estrogen biosynthesis
    • Osawa Y, Nakamura T (1982). Anti-human placental aromatase II cytochrome P-450 antibody and immunochemical study of estrogen biosynthesis. Endocrinology 110S:A-31.
    • (1982) Endocrinology , vol.110 S
    • Osawa, Y.1    Nakamura, T.2
  • 5
    • 0017088267 scopus 로고
    • Some properties of a detergent-solubilized NADPH-cytochrome C (cytochrome P-450) reductase purified by biospecific affinity chromatography
    • Yasukochi Y, Masters BSS (1976). Some properties of a detergent-solubilized NADPH-cytochrome C (cytochrome P-450) reductase purified by biospecific affinity chromatography. J Biol Chem 251: 5337-5344.
    • (1976) J Biol Chem , vol.251 , pp. 5337-5344
    • Yasukochi, Y.1    Masters, B.S.S.2
  • 6
    • 0025872595 scopus 로고
    • Purification of human placental aromatase cytochrome P-450 with monoclonal antibody and its characterization
    • Yoshida N, Osawa Y (1991). Purification of human placental aromatase cytochrome P-450 with monoclonal antibody and its characterization. Biochemistry 30:3003-3010.
    • (1991) Biochemistry , vol.30 , pp. 3003-3010
    • Yoshida, N.1    Osawa, Y.2
  • 8
    • 0017833104 scopus 로고
    • Purification of cytochrome P-450 and P-448 from rat liver microsomes
    • Ryan D, Lu AYH, Levin W (1978). Purification of cytochrome P-450 and P-448 from rat liver microsomes. Methods Enzymol 52: 117-123.
    • (1978) Methods Enzymol , vol.52 , pp. 117-123
    • Ryan, D.1    Lu, A.Y.H.2    Levin, W.3
  • 9
    • 50449100139 scopus 로고
    • The carbon monoxide binding pigment of liver microsomes
    • Omura T, Sato R (1964). The carbon monoxide binding pigment of liver microsomes. J Biol Chem 239:2379-2385.
    • (1964) J Biol Chem , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 227:680-683.
    • (1970) Nature (Lond) , vol.227 , pp. 680-683
    • Laemmli, U.K.1
  • 11
    • 0020324568 scopus 로고
    • Multiple forms of aromatase and response of breast cancer aromatase to antiplacental aromatase II antibodies
    • Osawa Y, Tochigi B, Higashiyama T, Yarborough C, Nakamura T, Yamamoto T (1982). Multiple forms of aromatase and response of breast cancer aromatase to antiplacental aromatase II antibodies. Cancer Res 42:3299s-3306s.
    • (1982) Cancer Res , vol.42
    • Osawa, Y.1    Tochigi, B.2    Higashiyama, T.3    Yarborough, C.4    Nakamura, T.5    Yamamoto, T.6
  • 12
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Köehler G, Milstein C (1975). Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256:495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Köehler, G.1    Milstein, C.2
  • 13
    • 0014504385 scopus 로고
    • General methods for the study of cells and serum during the immune response: The response to dinitrophenyl in mice
    • Klinman NR, Taylor RB (1969). General methods for the study of cells and serum during the immune response: The response to dinitrophenyl in mice. Clin Exp Immunol 4:473-487.
    • (1969) Clin Exp Immunol , vol.4 , pp. 473-487
    • Klinman, N.R.1    Taylor, R.B.2
  • 14
    • 77049138167 scopus 로고
    • The colorimetric estimation of formaldehyde by means of the Hantzsch reaction
    • Nash T (1953). The colorimetric estimation of formaldehyde by means of the Hantzsch reaction. Biochem J 55:416-421.
    • (1953) Biochem J , vol.55 , pp. 416-421
    • Nash, T.1
  • 16
    • 0342306530 scopus 로고
    • Species difference of ovarian aromatase recognized by a monoclonal antibody
    • Tochigi B, Tochigi M, Yoshida T, Tagaki S, Yarborough C (1986). Species difference of ovarian aromatase recognized by a monoclonal antibody. Endocrinology 118S:71, A-161.
    • (1986) Endocrinology , vol.118 S , pp. 71
    • Tochigi, B.1    Tochigi, M.2    Yoshida, T.3    Tagaki, S.4    Yarborough, C.5
  • 17
    • 0022475441 scopus 로고
    • Purification to homogeneity of aromatase from human placenta
    • Nakajin S, Shinoda M, Hall PF (1986). Purification to homogeneity of aromatase from human placenta. Biochem Biophys Res Commun 134:704-710.
    • (1986) Biochem Biophys Res Commun , vol.134 , pp. 704-710
    • Nakajin, S.1    Shinoda, M.2    Hall, P.F.3
  • 18
    • 0022492858 scopus 로고
    • Purification and reconstitution properties of human placental aromatase. A cytochrome P-450-type monooxygenase
    • Tan L, Muto N (1986). Purification and reconstitution properties of human placental aromatase. A cytochrome P-450-type monooxygenase. Eur J Biochem 156:243-250.
    • (1986) Eur J Biochem , vol.156 , pp. 243-250
    • Tan, L.1    Muto, N.2
  • 19
    • 0023266093 scopus 로고
    • Human placenta estrogen synthetase (aromatase) purified by affinity chromatography
    • Hagerman DD (1987). Human placenta estrogen synthetase (aromatase) purified by affinity chromatography. J Biol Chem 262: 2398-2400.
    • (1987) J Biol Chem , vol.262 , pp. 2398-2400
    • Hagerman, D.D.1
  • 20
    • 0023180688 scopus 로고
    • Purification and characterization of human placental aromatase cytochrome P-450
    • Kellis JT, Vickery LE (1987). Purification and characterization of human placental aromatase cytochrome P-450. J Biol Chem 262: 4413-4420.
    • (1987) J Biol Chem , vol.262 , pp. 4413-4420
    • Kellis, J.T.1    Vickery, L.E.2
  • 21
    • 0023949565 scopus 로고
    • Novel properties of human placental aromatase as cytochrome P-450: Purification and characterization of a unique form of aromatase
    • Harada N (1988). Novel properties of human placental aromatase as cytochrome P-450: Purification and characterization of a unique form of aromatase. J Biochem 103:106-113.
    • (1988) J Biochem , vol.103 , pp. 106-113
    • Harada, N.1
  • 22
    • 0024542732 scopus 로고
    • An enzyme-linked immunosorbent assay for quantitation of aromatase cytochrome P-450
    • Kitawaki J, Yoshida N, Osawa Y (1989). An enzyme-linked immunosorbent assay for quantitation of aromatase cytochrome P-450. Endocrinology 124:1417-1423.
    • (1989) Endocrinology , vol.124 , pp. 1417-1423
    • Kitawaki, J.1    Yoshida, N.2    Osawa, Y.3
  • 23
    • 38249034623 scopus 로고
    • Aromatase isozyme in goldfish brain and stereochemistry of the aromatization
    • Kitawaki J, Osawa Y, Callard GV (1987). Aromatase isozyme in goldfish brain and stereochemistry of the aromatization. Steroids 50:4-6.
    • (1987) Steroids , vol.50 , pp. 4-6
    • Kitawaki, J.1    Osawa, Y.2    Callard, G.V.3
  • 24
    • 0023468901 scopus 로고
    • Immunoaffinity purification of aromatase cytochrome P-450 from human placental microsomes, metabolic switching from aromatization to 1β and 2β-monohydroxylation, and recognition of aromatase isozymes
    • Osawa Y, Yoshida N, Fronckowiak M, Kitawaki J (1987). Immunoaffinity purification of aromatase cytochrome P-450 from human placental microsomes, metabolic switching from aromatization to 1β and 2β-monohydroxylation, and recognition of aromatase isozymes. Steroids 50:11-28.
    • (1987) Steroids , vol.50 , pp. 11-28
    • Osawa, Y.1    Yoshida, N.2    Fronckowiak, M.3    Kitawaki, J.4
  • 25
    • 0027314085 scopus 로고
    • Multiple functions of aromatase and the active site structure; aromatase is the placental estrogen 2-hydroxylase
    • Osawa Y, Higashiyama T, Shimizu Y, Yarborough C (1993). Multiple functions of aromatase and the active site structure; aromatase is the placental estrogen 2-hydroxylase. J Steroid Biochem Mol Biol 44:469-480.
    • (1993) J Steroid Biochem Mol Biol , vol.44 , pp. 469-480
    • Osawa, Y.1    Higashiyama, T.2    Shimizu, Y.3    Yarborough, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.