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Chemistry

D-Index
41
Citations
9088
World Ranking
17669
National Ranking
397

Overview

Burt Zerner was affiliated with the University of Queensland in Australia. Their work spanned multiple interdisciplinary fields, with a primary focus on Nursing and Environmental Science, reflecting a career that integrated health and environmental perspectives.

The scientist contributed to subfields including Nutrition and Dietetics as well as Health, Toxicology and Mutagenesis, indicating a diverse research approach addressing both nutritional health and the biological impacts of toxic substances.

The main topics of Burt Zerner's research concerned Trace Elements in Health and Chromium effects and bioremediation. These topics highlight an interest in the health implications of trace elements as well as environmental remediation involving chromium contamination.

Frequent collaborations were a feature of their research, with notable coauthors including:

  • Robert K. Andrews
  • Robert L. Blakeley

No records of recent papers or frequent publication venues were documented, nor any book publications from the available data.

Best Publications

  • Reassessment of Ellman's reagent.

    Peter W. Riddles;Robert L. Blakeley;Burt Zerner

  • Ellman's reagent: 5,5'-dithiobis(2-nitrobenzoic acid)--a reexamination.

    Peter W. Riddles;Robert L. Blakeley;Burt Zerner

  • JACK BEAN UREASE (EC 3.5.1.5), A METALLOENZYME, A SIMPLE BIOLOGICAL ROLE FOR NICKEL

    Nicholas E. Dixon;Carlo Gazzola;Robert L. Blakeley;Burt Zerner

  • Jack bean urease (EC 3.5.1.5). V. On the mechanism of action of urease on urea, formamide, acetamide, N-methylurea, and related compounds

    Nicholas E. Dixon;Peter W. Riddles;Carlo Gazzola;Robert L. Blakeley

  • Jack bean urease: the first nickel enzyme

    Robert L. Blakeley;Burt Zerner

  • Kinetic Evidence for the Formation of Acyl-Enzyme Intermediates in the -Chymotrypsin-Catalyzed Hydrolyses of Specific Substrates

    Burt. Zerner;Richard P. M. Bond;Myron L. Bender

  • Recent advances in the chemistry of an old enzyme, urease

    Burt Zerner

  • The Kinetic Consequences of the Acyl-Enzyme Mechanism for the Reactions of Specific Substrates with Chymotrypsin

    Burt. Zerner;Myron L. Bender

  • Properties of a purple phosphatase from red kidney bean: a zinc-iron metalloenzyme

    Jennifer L. Beck;Lyndal A. McConachie;Andrew C. Summors;Wilfred N. Arnold

  • Jack bean urease (EC 3.5.1.5). III. The involvement of active-site nickel ion in inhibition by beta-mercaptoethanol, phosphoramidate, and fluoride.

    Nicholas E. Dixon;Robert L. Blakeley;Burt Zerner

  • Jack bean urease (EC 3.5.1.5). IV. The molecular size and the mechanism of inhibition by hydroxamic acids. Spectrophotometric titration of enzymes with reversible inhibitors.

    Nicholas E. Dixon;John A. Hinds;Ann K. Fihelly;Carlo Gazzola

  • Jack bean urease (EC 3.5.1.5). Demonstration of a carbamoyl-transfer reaction and inhibition by hydroxamic acids

    Robert L. Blakeley;John A. Hinds;Hugo E. Kunze;Edwin C. Webb

  • Iron-containing acid phosphatases: Comparison of the enzymes from beef spleen and pig allantoic fluid

    Hugh D. Campbell;David A. Dionysius;Dianne T. Keough;Bruce E. Wilson

  • Jack bean urease (EC 3.5.1.5). A new purification and reliable rate assay

    Robert L. Blakeley;Edwin C. Webb;Burt Zerner

  • Spectrophotometric Investigations of the Mechanism of α-Chymotrypsin-catalyzed Hydrolyses. Detection of the Acyl-enzyme Intermediate1-3

    Myron L. Bender;Gregory R. Schonbaum;Burt. Zerner

  • Nickel(II)-promoted ethanolysis and hydrolysis of N-(2-pyridylmethyl)urea. A model for urease

    Robert L. Blakeley;Anthony Treston;Robert K. Andrews;Burt Zerner

  • Inhibition of Jack Bean urease (EC 3.5.1.5) by acetohydroxamic acid and by phosphoramidate. An equivalent weight for urease.

    Nicholas E. Dixon;Carlo Gazzola;James J. Watters;Robert L. Blakeley

  • Metal ions in enzymes using ammonia or amides

    Nicholas E. Dixon;Carlo Gazzola;Robert L. Blakeley;Burt Zerner

  • Carboxylesterases (EC 3.1.1). Kinetic studies on carboxylesterases.

    James K. Stoops;Douglas J. Horgan;Maria T. C. Runnegar;John De Jersey

  • Mössbauer analysis of the binuclear iron site in purple acid phosphatase from pig allantoic fluid

    J. T Sage;Y. M. Xia;P. G. Debrunner;D. T. Keough

Frequent Co-Authors

Myron L. Bender
Myron L. Bender Northwestern University
Nicholas E. Dixon
Nicholas E. Dixon University of Wollongong
Michael P. Hendrich
Michael P. Hendrich Carnegie Mellon University
Charles J. O'Connor
Charles J. O'Connor University of New Orleans
Susan L. Hamilton
Susan L. Hamilton Baylor College of Medicine

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