Robert W. Benson

Environmental Protection Agency

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Dean W. Roberts

University of Arkansas for Medical Sciences

Neil R. Pumford

AbbVie (United States)

David W. Potter

Allogene Therapeutics (United States)

Fred F. Kadlubar

University of Arkansas for Medical Sciences

J. A. Hinson

University of Arkansas for Medical Sciences

Paul D. Boyer

Cornell University

R. S. Speirs

Prostate Cancer Foundation of Australia

John Snawder

National Institute for Occupational Safety and Health

Thomas J. Flammang

National Center for Toxicological Research

Jack Hinson

University of Arkansas for Medical Sciences

Cooperative Institutions

National Center for Toxicological Research

United States Food and Drug Administration

University of Arkansas for Medical Sciences

University of Arkansas at Little Rock

National Institutes of Health

Arkansas Children's Hospital

Northeastern University

Food and Drug Administration

University of Minnesota

National Cancer Institute

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The Participation of an Enzyme-bound Oxygen Group in a Coenzyme A Transferase Reaction

Journal of Biological Chemistry (1969)

Robert W. Benson Paul D. Boyer

Abstract A well supported mechanism for succinyl-CoA:3-ketoacid coenzyme A transferase (EC 2.8.3.5) involving an enzyme-CoA intermediate requires the participation of an oxygen atom of the enzyme or of the CoA moiety. Measurements of loss of 18O from acetoacetate show that CoA oxygens do not participate. An oxygen-containing group on the enzyme is reversibly labeled from succinate-18O in the presence of acetoacetyl-CoA or succinyl-CoA. The 18O-labeled enzyme does not contain succinyl or CoA moieties. A binding of acetoacetate-14C to the enzyme preparation does not appear to reflect an anhydride precursor to the enzyme-CoA form.

Coenzyme A

Transferase

Moiety

Acetyl-CoA

10.1016/s0021-9258(19)78234-9

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Citations (15)

Immunological homology among azoreductases from Clostridium and Eubacterium strains isolated from human intestinal microflora

Journal of Basic Microbiology (1992)

Fatemeh Rafii Don B. Smith Robert W. Benson Carl E. Cerniglia

Abstract Azoreductases from several anaerobic intestinal bacteria have been shown to reduce azo dyes to carcinogenic aromatic amines. To evaluate the structural similarities of azoreductases from four species of Clostridium and one species of Eubacterium , a polyclonal antibody against purified Clostridium perfringens azoreductase was generated in rabbits. This antibody inhibited the azoreductase activity of all five bacteria tested. ELISA showed different degrees of binding of the antibody to various species of bacteria. In a Western blot, the antibody reacted with the purified azoreductases from all four Clostridium species and the Eubacterium species. These results demonstrate that the azoreductases from the bacteria tested share similar antigenic domains, which are probably located in the active site of the enzyme. Azoreductases from these intestinal bacteria are similar enough to be considered as a single group of enzymes with respect to their functions and antigenicity.

Eubacterium

Polyclonal antibodies

Clostridium perfringens

Antigenicity

Peptostreptococcus

10.1002/jobm.3620320204

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Mutagenicity and carcinogenicity in relation to DNA adduct formation in rats fed leucomalachite green

Mutation Research/Fundamental and Molecular Mechanisms of Mutagenesis (2002)

Sandra J. Culp Frederick A. Beland Robert H. Heflich Robert W. Benson Lonnie R. Blankenship

Malachite green

10.1016/s0027-5107(02)00152-5

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Immunochemical quantitation of 3-(cystein-S-yl)acetaminophen adducts in serum and liver proteins of acetaminophen-treated mice.

Journal of Pharmacology and Experimental Therapeutics (1989)

Neil R. Pumford J A Hinson David W. Potter K L Rowland Robert W. Benson

Using a recently developed enzyme-linked immunosorbent assay specific for 3-(cystein-S-yl)acetaminophen adducts we have quantitated the formation of these specific adducts in liver and serum protein of B6C3F1 male mice dosed with acetaminophen. Administration of acetaminophen at doses of 50, 100, 200, 300, 400 and 500 mg/kg to mice resulted in evidence of hepatotoxicity (increase in serum levels of alanine aminotransferase and aspartate aminotransferase) at 4 hr in the 300, 400 and 500 mg/kg treatment groups only. The formation of 3-(cystein-S-yl)acetaminophen adducts in liver protein was not observed in the groups receiving 50, 100 and 200 mg/kg doses, but was observed in the groups receiving doses above 300 mg/kg of acetaminophen. Greater levels of adduct formation were observed at the higher doses. 3-(Cystein-S-yl)acetaminophen protein adducts were also observed in serum of mice receiving hepatotoxic doses of acetaminophen. After a 400 mg/kg dose of acetaminophen, 3-(cystein-S-yl)acetaminophen adducts in the liver protein reached peak levels 2 hr after dosing. By 12 hr the levels decreased to approximately 10% of the peak level. In contrast, 3-(cystein-S-yl)acetaminophen adducts in serum protein were delayed, reaching a sustained peak 6 to 12 hr after dosing. The dose-response correlation between the appearance of serum aminotransferases and 3-(cystein-S-yl)acetaminophen adducts in serum protein and the temporal correlation between the decrease in 3-(cystein-S-yl)acetaminophen adducts in liver protein and the appearance of adducts in serum protein are consistent with a hepatic origin of the adducts detected in serum protein.(ABSTRACT TRUNCATED AT 250 WORDS)

Acetaminophen

10.1016/s0022-3565(25)23630-8

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Immunochemical quantitation of DNA adducts derived from the human bladder carcinogen 4-aminobiphenyl.

PubMed (1988)

Dean W. Roberts Robert W. Benson John D. Groopman Thomas J. Flammang William A. Nagle

To assess target-tissue exposure to the human urinary bladder carcinogen 4-aminobiphenyl (ABP), we have developed a sensitive immunochemical method for measuring the major arylamine-DNA adduct formed, N-(guan-8-yl)-ABP (Gua-C8-ABP). High-affinity polyclonal antisera from rabbits immunized with N-(guanosin-8-yl)-ABP coupled to keyhole limpet hemocyanin were characterized and shown to have high specificity for antigenic determinants on the purine and biphenyl rings of Gua-C8-ABP and minimal cross-reactivity with ABP, deoxyguanosine, or hydrolyzed DNA. Assay standards containing ABP-modified DNA were prepared by reacting [3H]N-hydroxy-ABP with calf thymus DNA. DNA samples were hydrolyzed with trifluoroacetic acid and dried under vacuum, and the residues were dissolved in dimethyl sulfoxide under argon. Using a streptavidin-biotin amplified enzyme-linked immunosorbent assay, DNA hydrolysates competed at 25 micrograms DNA/microtiter well for a limiting amount of anti-keyhole limpet hemocyanin-(Gua-C8-ABP) in the presence of excess solid-phase bovine serum albumin-(Gua-C8-ABP) coating antigen. The limit of sensitivity for this assay using 25 micrograms DNA was 2 adducts/10(8) nucleotides. Gua-C8-ABP adducts in liver and bladder epithelial DNAs were readily quantified after p.o. administration of 5 mg/kg ABP to dogs. This methodology is capable of detecting adducts at levels of biological significance and should be applicable to human target-tissue dosimetry.

Keyhole limpet hemocyanin

Deoxyguanosine

Lactoperoxidase

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Citations (25)

Mechanical Hysteresis

The Journal of the Acoustical Society of America (1963)

Robert W. Benson

Hysteresis loops have been obtained on metallic samples vibrated at large-strain amplitudes at rates of several kilocycles per second. The mechanical-hysteresis loop is of the form of an asymmetrical “figure 8” pattern. The cause of the asymmetry is discussed relative to transducer design and also its effect upon fatigue life. Related experiments have been performed that indicate the importance of lateral motions of transducing elements in determining loss characteristics of vibrating solids. The study has led to methods for the prediction of the onset of a marked increase in loss with strain amplitude and also the onset of a catastrophic increase in loss leading to failure by fatigue. [This work was conducted under sponsorship of the U. S. Office of Naval Research.]

Hysteresis

10.1121/1.2142734

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Simultaneous stabilization using genetic algorithms

OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (1991)

Robert W. Benson W. E. Schmitendorf

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Direct and ¹⁸O-Exchange Measurements Relevant to Possible Activated or Phosphorylated States of Myosin^*

Biochemistry (1966)

L. Sartorelli Herbert J. Fromm Robert W. Benson Paul D. Boyer

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDirect and 18O-Exchange Measurements Relevant to Possible Activated or Phosphorylated States of Myosin*L. Sartorelli, H. J. Fromm, R. W. Benson, and P. D. BoyerCite this: Biochemistry 1966, 5, 9, 2877–2884Publication Date (Print):September 1, 1966Publication History Published online1 May 2002Published inissue 1 September 1966https://pubs.acs.org/doi/10.1021/bi00873a015https://doi.org/10.1021/bi00873a015research-articleACS PublicationsRequest reuse permissionsArticle Views31Altmetric-Citations45LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

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10.1021/bi00873a015

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Citations (54)

How Judges Fool Themselves

Springer eBooks (1988)

Robert W. Benson

10.1007/978-1-4613-0771-6_3

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Citations (1)

Cultural Resources Survey of the Proposed SR 14 Bridge Replacement Over Noland Creek, Autauga County, Alabama

Robert W. Benson Ken Kocher

Bridge (graph theory)

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