Sang S. Park

Seoul National University

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H V Gelboin

National Cancer Institute

Byeong Jun Song

Myongji Hospital

T Fujino

Saitama Medical University

Frank J. Gonzalez

National Institutes of Health

Fred K. Friedman

Duke Cancer Institute

Chung S. Yang

Rutgers, The State University of New Jersey

Hasan Mukhtar

University of Wisconsin–Madison

Waydell Walker

National Cancer Institute

Yun-Lian Lin

China Medical University

Kui Cheng

Southern Medical University

Cooperative Institutions

National Cancer Institute

National Institutes of Health

Rutgers, The State University of New Jersey

Rutgers New Jersey Medical School

National Yang Ming Chiao Tung University

National Research Institute of Chinese Medicine

Center for Cancer Research

Seoul National University

University of Wisconsin–Madison

Ministry of Health and Welfare

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Detection and purification of cytochromes P-450 in animal tissues with monoclonal antibodies.

Journal of Biological Chemistry (1984)

Kui Cheng H V Gelboin Byeong Jun Song Sang S. Park Fred K. Friedman

Monoclonal antibody (MAb)-based radioimmunoassay (RIA) and immunopurification procedures were used to probe the immunochemical relatedness of cytochromes P-450 in tissues from different species. RIAs based on MAb 1-7-1 and MAb 1-31-2, both to the major 3-methylcholanthrene (MC)-induced rat liver microsomal cytochrome P-450, detected antigenically related forms of cytochrome P-450 in liver microsomes from MC-induced rats, C57BL/6 and DBA/2 mice, hamsters, and guinea pigs, and in lung and kidney microsomes of MC-induced rats. Individual cytochromes P-450 were also isolated from these microsomes by MAb-directed immunopurification. When bound to Sepharose, MAb 1-7-1 adsorbed two species of Mr 56,000 and 57,000 from liver microsomes from rats and C57BL/6 mice, while MAb 1-31-2 adsorbed only the Mr 57,000 polypeptide. These results reveal that livers from both rats and C57BL/6 mice contain a cytochrome P-450 (Mr 56,000) with the epitope for 1-7-1 and a cytochrome P-450 (Mr 57,000) with epitopes for both 1-31-2 and 1-7-1. Additional immunochemical relatedness between the cytochromes P-450 in different tissues was demonstrated by MAb-directed immunopurification of cytochromes P-450 from DBA/2 mouse liver (Mr 56,000), guinea pig liver (Mr 53,000), hamster liver (Mr 57,000), and rat lung (Mr 57,000). These results demonstrate the efficacy of MAb-based RIA and immunopurification procedures for simple and rapid detection and purification of cytochromes P-450 from a variety of tissues.

10.1016/s0021-9258(20)71351-7

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Citations (48)

Monoclonal antibodies to rat liver microsomal cytochrome b5

Biochemical Pharmacology (1992)

Sang S. Park Waydell Walker Toshifumi Aoyama D P Lapenson David J. Waxman

Cytochrome b5

Ouchterlony double immunodiffusion

10.1016/0006-2952(92)90179-m

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Citations (6)

Effects of baicalein and wogonin on drug-metabolizing enzymes in C57BL/6J mice

Life Sciences (2000)

Yune‐Fang Ueng Chi-Chuo Shyu Yun-Lian Lin Sang S. Park Jyh‐Fei Liao

Baicalein

Wogonin

CYP3A

Baicalin

Demethylation

10.1016/s0024-3205(00)00809-2

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Citations (36)

Monoclonal Antibodies Directed Characterization of Epidermal and Hepatic Cytochrome P-450 Isozymes Induced by Skin Application of Therapeutic Crude Coal Tar

Journal of Investigative Dermatology (1989)

Wasiuddin A. Khan Sang S. Park Harry V. Gelboin David R. Bickers Hasan Mukhtar

Phenobarbital

10.1111/1523-1747.ep12277342

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Citations (20)

Monoclonal antibody-directed radioimmunoassay of specific cytochromes P-450.

Journal of Biological Chemistry (1984)

Byeong Jun Song T Fujino Sang S. Park Fred K. Friedman H V Gelboin

A rapid solid phase radioimmunoassay (RIA) for cytochromes P-450 has been developed utilizing specific monoclonal antibodies to major forms of rat liver cytochrome P-450 that are induced by 3-methylcholanthrene (MC-P-450) and phenobarbital (PB-P-450). Monoclonal antibodies (MAbs) that were endogenously labeled with [35S]methionine were used to detect MAb-specific cytochromes P-450 in liver microsomes from untreated rats and rats pretreated with 3-methylcholanthrene (MC) or phenobarbital. The competitive binding assays are rapid and can detect cytochrome P-450 in less than 100 ng of microsomal protein. The RIA was used to examine the distribution of MAb-specific cytochromes P-450 in extrahepatic tissues of MC-treated rats; an approximately 30- to 50-fold greater amount of MC-P-450 in liver relative to lung and kidney was observed, which corresponds well with aryl hydrocarbon hydroxylase activity in these tissues. The inducibility of MAb-specific cytochromes P-450 in several species was also examined by competitive RIA. Significant increases in the MAb-specific P-450 were observed in MC-treated rats, guinea pigs, and C57BL/6 mice, all highly inducible for aryl hydrocarbon hydroxylase; little increase was observed for the relatively noninducible DBA/2 mouse strain.

Phenobarbital

Methylcholanthrene

10.1016/s0021-9258(17)43417-x

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Citations (31)

Monoclonal antibody-directed phenotyping of cytochrome P-450-dependent aryl hydrocarbon hydroxylase and 7-ethoxycoumarin deethylase in mammalian tissues.

Journal of Biological Chemistry (1984)

T Fujino Donna West Sang S. Park Harry V. Gelboin

The distribution of cytochromes P-450 that catalyze aryl hydrocarbon hydroxylase and 7-ethoxycoumarin O-deethylase were studied with monoclonal antibody (MAb) 1-7-1 which completely inhibits these activities of a purified 3-methylcholanthrene-induced rat liver cytochrome P-450. The degree of inhibition by MAb 1-7-1 quantitatively assesses the contribution of different cytochromes P-450 in the liver, lung, and kidney microsomes from untreated, 3-methylcholanthrene- and phenobarbital (PB)-treated rats, mice, guinea pigs, and hamsters. Enzyme sensitivity to MAb 1-7-1 inhibition defines two types of cytochrome P-450 contributing to aryl hydrocarbon hydroxylase and 7-ethoxycoumarin O-deethylase. The MAb 1-7-1-sensitive cytochrome P-450 is a major contributor to aryl hydrocarbon hydroxylase in rat liver, lung, and kidney of 3-methylcholanthrene-treated rats, C57BL/6 mice, guinea pigs, and hamsters; this type is also present in lesser amounts in the extrahepatic tissues of the control and PB-treated animals, and in the lungs of the relatively noninducible DBA/2 mice treated with 3-methylcholanthrene. This form however makes little or no contribution to liver aryl hydrocarbon hydroxylase of control or PB-treated animals. 7-Ethoxycoumarin O-deethylase is also a function of both the MAb 1-7-1-sensitive and insensitive classes of cytochrome P-450. The ratio of the classes contributing to aryl hydrocarbon hydroxylase and 7-ethoxycoumarin O-deethylase differs in the various tissues and species and after inducer treatment. All of the 7-ethoxycoumarin O-deethylase activity in guinea pigs and hamsters is a function of cytochromes P-450 different than the MAb 1-7-1-sensitive cytochrome P-450 responsible for aryl hydrocarbon hydroxylase activity. Thus, the MAb 1-7-1 antigenically defines the type of cytochromes P-450 contributing to each reaction. Cytochromes P-450 can be viewed as paradigmatic for enzyme systems in which the nature and amount of product is regulated by multiple isoenzymic forms. Analyses using monoclonal antibodies to specific isoenzymes may thus have broad application to a variety of other complex systems which are composed of multiple isoenzymes.

Phenobarbital

Methylcholanthrene

10.1016/s0021-9258(17)47262-0

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Citations (39)

Mechanism of induction of cytochrome P-450ac (P-450j) in chemically induced and spontaneously diabetic rats

Archives of Biochemistry and Biophysics (1988)

Zigong Dong Jun‐Yan Hong Qiang Ma Dechun Li John Bullock

Alloxan

Demethylase

10.1016/0003-9861(88)90610-8

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Citations (142)