Johnson Research Foundation Research Articles

WHAT I LEARNED FROM BRITTON CHANCE

In this personal and reflective article, I honor the memory of Britton Chance and explain how his mentorship during my tenure at the Johnson Research Foundation greatly impacted my scientific career. I emphasize the critical role of mentors on the development of scientists and present some wonderful and remarkable attributes that characterized Britton Chance's scientific and personal style.

Anesthesiology: From Patient Safety to Population Outcomes

Anesthesiology: From Patient Safety to Population Outcomes

Britton Chance (1913–2010)

A pioneering scientist and gold medal Olympian had unflagging energy and broad interests that fueled his research.

Forty-Three Years Ago in Philadelphia

Dear Dr. Estabrook,This short note is the recollections of my stay in your laboratory at the Johnson Research Foundation in the University of Pennsylvania in 1964–1965. It was more than 40 years ag...

Design of a Synthetic Receptor for the Calmodulin-Binding Domain of Calcineurin

ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTDesign of a Synthetic Receptor for the Calmodulin-Binding Domain of CalcineurinAngela Lombardi, James W. Bryson, Giovanna Ghirlanda, and William F. DeGradoView Author Information Centro Interuniversitario di Ricerca sui Peptidi Bioattivi & Centro di Studio di Biocristallografia del C.N.R University of Naples “Federico II” Via Mezzocannone 4, I-80134 Naples, Italy Ecogen Inc., 2005 Cabot Blvd. West Langhorne, Pennsylvania 19047 The Johnson Research Foundation Department of Biochemistry and Biophysics University of Pennsylvania Philadelphia, Pennsylvania 19104-6059 Cite this: J. Am. Chem. Soc. 1997, 119, 50, 12378–12379Publication Date (Web):December 17, 1997Publication History Received25 August 1997Published online17 December 1997Published inissue 17 December 1997https://doi.org/10.1021/ja972973dCopyright © 1997 American Chemical SocietyRIGHTS & PERMISSIONSArticle Views205Altmetric-Citations15LEARN 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 InReddit Read OnlinePDF (169 KB) Get e-AlertsSupporting Info (1)»Supporting Information Supporting Information SUBJECTS:Chemical structure,Mathematical methods,Oligomers,Peptides and proteins,Receptors Get e-Alerts

A Designed Buried Salt Bridge in a Heterodimeric Coiled Coil

ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTA Designed Buried Salt Bridge in a Heterodimeric Coiled CoilJoel P. Schneider, James D. Lear, and William F. DeGradoView Author Information The Johnson Research Foundation Department of Biochemistry & Biophysics University of Pennsylvania Philadelphia, Pennsylvania 19104-6059 Cite this: J. Am. Chem. Soc. 1997, 119, 24, 5742–5743Publication Date (Web):June 18, 1997Publication History Received17 February 1997Published online18 June 1997Published inissue 1 June 1997https://doi.org/10.1021/ja970493gCopyright © 1997 American Chemical SocietyRIGHTS & PERMISSIONSArticle Views473Altmetric-Citations61LEARN 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 InReddit Read OnlinePDF (118 KB) Get e-AlertsSupporting Info (1)»Supporting Information Supporting Information SUBJECTS:Chemical specificity,Free energy,Noncovalent interactions,Peptides and proteins,Salts Get e-Alerts

Binding of Halothane to Serum Albumin: Relevance to Theories of Narcosis

Departments of Anesthesiology and the Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104.In Reply:--Eger and Koblin raise several issues concerning the validity of albumin as a model to study mechanisms of inhalational anesthetic action and the relevance of the concentrations both of halothane and diethyl ether used in our studies. The principal aim of our communication was to describe an alternative and useful approach to determining anesthetic-protein interactions. Albumin was selected to compare the tryptophan fluorescence quenching method with the previous studies on anesthetic binding to this protein, which used19F-NMR and photoaffinity labeling. Our experiments were performed at 25 degrees Celsius to permit comparison with the earlier studies conducted at similar temperatures and because the direct information available suggests that, at least over the temperature range from 5 degrees Celsius to 20 degrees Celsius, volatile general anesthetic binding to protein targets only changes by 20–30%.The measured dissociation constants of halothane and diethyl ether determined using quenching of tryptophan fluorescence are greater than those required to maintain the anesthetic state in animals. It would be remarkable if the anesthetic binding sites on albumin exactly reproduced the clinical pharmacology of the inhaled general anesthetics. However, the fact that these tryptophan domains bind anesthetics within an order of magnitude of their clinical ED50's suggests that they may share some characteristics with the physiologically relevant sites. Although this was not the primary goal of the work, this is a satisfactory first approximation, because a tenfold change in affinity only corresponds to a binding energy of 1.4 kcal/mol (comparable to a single hydrogen bond ). Our study opens the door methodologically for a molecular description of anesthetic binding sites in proteins: For example, one avenue would be the use of site-directed mutagenesis of the albumin sites to conduct a structure-affinity study with a variety of volatile anesthetic molecules.In further response to the points made by Eger and Koblin concerning the weakness of the binding and the failure to reproduce the relative order of potencies seen clinically, it should be emphasized that it remains to be established that these structurally diverse molecules act at a single locus. Furthermore, it is far from clear that clinical EC50values must correspond directly to experimental dissociation constants. These questions remain unanswered, because the methodology to directly study volatile anesthetic binding has been unavailable until recently and is under development. Binding studies accounting for anesthetic desolvation and the formation of interactions with protein sites with a focus on molecular structure are needed. Using our approach and other techniques, the answers to these questions are forthcoming.Jonas S. Johansson, M.D., Ph.D., Roderic G. Eckenhoff, M.D., P. Leslie Dutton, F.R.S., Departments of Anesthesiology and the Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104.

Theo's Laboratory

The FASEB JournalVolume 9, Issue 8 p. 692-693 Milestones in Biological Research Theo's Laboratory Britton Chance, Corresponding Author Britton Chance n/a@.dne Address correspondence to Dr. Chance at: The Johnson Research Foundation, D501 Richards Building, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.Search for more papers by this author Britton Chance, Corresponding Author Britton Chance n/a@.dne Address correspondence to Dr. Chance at: The Johnson Research Foundation, D501 Richards Building, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.Search for more papers by this author First published: 01 May 1995 https://doi.org/10.1096/fasebj.9.8.7768363AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article. Volume9, Issue8May 1995Pages 692-693 RelatedInformation

In Pursuit of Protein Folding

Johnson Research Foundation, Department of Biochemistry and Biophysics, University ofPennsylvania School of Medicine, Philadelphia, PA 19104–6059Exploring the “Anfinsen trail,” the pathway by which unstructured proteins spontaneouslyfold to their native functional form, has become a central goal of the protein chemists. Inorder to understand a biochemical pathway, one wants to isolate and describe theintermediate structures that lead from precursor to product. Unfortunately the intermediateforms that define protein folding pathways cannot be isolated or studied by the usualmethodologies, however powerful, because folding intermediates are by definition unstable.Nevertheless, two reports in this issue, one by Miranker et al. on page 896, the other byJennings and Wright on page 892, are able to present fairly detailed structural informationon some kinetic folding intermediates in lysozyme and myoglobin, even though theseephemera only exist for less than 1 s during the folding process (1, 2). A related researcharticle by Mayo and Baldwin on page 873 describes some characteristics of equilibriumunfolding intermediates in ribonuclease A that exist transiently at infinitesimal levels inequilibrium with the native state (3).The folding experiments depend on a recently developed method (4) to obtain kinetic andstructural information on partially folded protein forms that fly by on a millisecond timescale. The intermediates were labeled in-flight in a structurally sensitive way, in essence bywriting on them with a brief pulse of chemical spray paint at any given point of time duringfolding. The painting technology (see figure) relies on the naturally occurring exchange ofhydrogens between water and the peptide group NH hydrogens distributed uniformlythroughout every protein molecule (5).The protein in D

NAD/NADH: redox state changes on cat brain cortex during stimulation and hypercapnia

Page H619: Laszlo Gyulai, Eörs Dora, and Arisztid G. B. Kovach. “NAD/NADH: redox state changes on cat brain cortex during stimulation and hypercapnia.” Authors' affiliation line should read: Experimental Research Department and Second Institute of Physiology, Semmelweis Medical University, Budapest, Üllöi ut 78/a, Hungary. Address for reprint requests: L. Gyulai, Johnson Research Foundation, University of Pennsylvania, 37th and Hamilton Walk, Richards Bldg.Ü5th Floor, Philadelphia, PA 19104.

#17: NON-INVASIVE ASSESSMENT OF HIGH ENERGY PHOSPHATE METABOLISM IN EXERCISING MUSCLE USING NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Johnson Research Foundation and Sports Medicine Center, University of Pennsylvania School of Medicine, Phila., PA 19104

A transmembrane quinone pair in the succinate dehydrogenase‐cytochrome b region

FEBS LettersVolume 82, Issue 2 p. 179-182 Full-length articleFree Access A transmembrane quinone pair in the succinate dehydrogenase-cytochrome b region J.C. Salerno, J.C. Salerno Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorH.J. Harmon, H.J. Harmon Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorHaywood Blum, Haywood Blum Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorJ.S. Leigh, J.S. Leigh Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorTomoko Ohnishi, Tomoko Ohnishi Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this author J.C. Salerno, J.C. Salerno Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorH.J. Harmon, H.J. Harmon Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorHaywood Blum, Haywood Blum Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorJ.S. Leigh, J.S. Leigh Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this authorTomoko Ohnishi, Tomoko Ohnishi Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USASearch for more papers by this author First published: October 15, 1977 https://doi.org/10.1016/0014-5793(77)80579-6Citations: 55AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume82, Issue2October 15, 1977Pages 179-182 ReferencesRelatedInformation

Alcohol and Aldehyde Metabolizing Systems. Papers Presented at the First International Symposium on Alcohol and Aldehyde Metabolizing Systems in Stockholm, Sweden, July 9-11, 1973. Johnson Research Foundation Colloquia Academic Press Rapid Manuscript Reproduction.Ronald G. Thurman, Takashi, Yonetani, John R. Williamson

Previous articleNext article No AccessNew Biological BooksAlcohol and Aldehyde Metabolizing Systems. Papers Presented at the First International Symposium on Alcohol and Aldehyde Metabolizing Systems in Stockholm, Sweden, July 9-11, 1973. Johnson Research Foundation Colloquia Academic Press Rapid Manuscript Reproduction. Ronald G. Thurman, Takashi, Yonetani, John R. WilliamsonKeith DalzielKeith Dalziel Search for more articles by this author PDFPDF PLUS Add to favoritesDownload CitationTrack CitationsPermissionsReprints Share onFacebookTwitterLinkedInRedditEmail SectionsMoreDetailsFiguresReferencesCited by The Quarterly Review of Biology Volume 50, Number 4Dec., 1975 Published in association with Stony Brook University Article DOIhttps://doi.org/10.1086/408778 Copyright 1975 Stony Brook Foundation, Inc.PDF download Crossref reports no articles citing this article.

Erratum: National Medal of Science Winners

In the box on the National Medal of Science Winners (11 July, page 121), Britton Chance's affiliation should be the Johnson Research Foundation, University of Pennsylvania.

Ethidium bromide as an uncoupler of oxidative phosphorylation

FEBS LettersVolume 54, Issue 3 p. 347-352 Full-length articleFree Access Ethidium bromide as an uncoupler of oxidative phosphorylation Milan Miko, Corresponding Author Milan Miko Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19104, USATo whom all correspondence should be addressed. Present address; Dept. of Microbiology and Biochemistry, Slovak Polyt. Univ., 880 37 Bratislava, Janska 1, Czechoslovakia.Search for more papers by this authorBritton Chance, Britton Chance Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19104, USASearch for more papers by this author Milan Miko, Corresponding Author Milan Miko Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19104, USATo whom all correspondence should be addressed. Present address; Dept. of Microbiology and Biochemistry, Slovak Polyt. Univ., 880 37 Bratislava, Janska 1, Czechoslovakia.Search for more papers by this authorBritton Chance, Britton Chance Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19104, USASearch for more papers by this author First published: July 01, 1975 https://doi.org/10.1016/0014-5793(75)80937-9Citations: 28AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume54, Issue3July 01, 1975Pages 347-352 ReferencesRelatedInformation

Optical, NMR and EPR properties of horseradish peroxidase and its donor complexes

FEBS LettersVolume 51, Issue 1-2 p. 304-308 Full-length articleFree Access Optical, NMR and EPR properties of horseradish peroxidase and its donor complexes J.S. Leigh, J.S. Leigh Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19174, USASearch for more papers by this authorM.M. Maltempo, M.M. Maltempo Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19174, USASearch for more papers by this authorP. I. Ohlsson, P. I. Ohlsson Department of Chemistry, University of Umeå, S-90187 Umeå, SwedenSearch for more papers by this authorK. G. Paul, K. G. Paul Department of Chemistry, University of Umeå, S-90187 Umeå, SwedenSearch for more papers by this author J.S. Leigh, J.S. Leigh Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19174, USASearch for more papers by this authorM.M. Maltempo, M.M. Maltempo Johnson Research Foundation, School of Medicine, University of Pennsylvania, Philadelphia, Pa. 19174, USASearch for more papers by this authorP. I. Ohlsson, P. I. Ohlsson Department of Chemistry, University of Umeå, S-90187 Umeå, SwedenSearch for more papers by this authorK. G. Paul, K. G. Paul Department of Chemistry, University of Umeå, S-90187 Umeå, SwedenSearch for more papers by this author First published: March 01, 1975 https://doi.org/10.1016/0014-5793(75)80913-6Citations: 44 Visiting Professor Johnson Foundation, 1974–1975. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume51, Issue1-2March 01, 1975Pages 304-308 ReferencesRelatedInformation

Kinetic studies on cytochrome b— c1 interaction in the isolated succinate-cytochrome c reductase

FEBS LettersVolume 24, Issue 3 p. 269-272 Full-length articleFree Access Kinetic studies on cytochrome b—c 1 interaction in the isolated succinate-cytochrome c reductase M. Erecińska, M. Erecińska Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this authorD.F. Wilson, D.F. Wilson Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this author M. Erecińska, M. Erecińska Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this authorD.F. Wilson, D.F. Wilson Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this author First published: August 15, 1972 https://doi.org/10.1016/0014-5793(72)80370-3Citations: 21AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume24, Issue3August 15, 1972Pages 269-272 ReferencesRelatedInformation

Temperature sensitivity of fluorescence probes in the presence of model membranes and mitochondria

FEBS LettersVolume 22, Issue 1 p. 23-26 Full-length articleFree Access Temperature sensitivity of fluorescence probes in the presence of model membranes and mitochondria J.M. Vanderkooi, J.M. Vanderkooi Department of Biophysics and Physical Biochemistry, Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this authorB. Chance, B. Chance Department of Biophysics and Physical Biochemistry, Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this author J.M. Vanderkooi, J.M. Vanderkooi Department of Biophysics and Physical Biochemistry, Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this authorB. Chance, B. Chance Department of Biophysics and Physical Biochemistry, Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USASearch for more papers by this author First published: April 15, 1972 https://doi.org/10.1016/0014-5793(72)80209-6Citations: 37AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume22, Issue1April 15, 1972Pages 23-26 ReferencesRelatedInformation

Nonideal Techniques: Probes of Structure and Function of Macromolecules and Membranes . Proceedings of a Johnson Research Foundation colloquium, Philadelphia, April 1969. Academic Press, New York, 1971. Vol. 1, Probes and Membrane Function. Britton Chance, Chuan-Pu Lee, and J. Kent Blasie, Eds. xxx, 552 pp., illus. $13.50. Vol. 2, Probes of Enzymes and Hemoproteins. Britton Chance, Takashi Yonetani, and Albert

Nonideal Techniques: <i>Probes of Structure and Function of Macromolecules and Membranes</i> . Proceedings of a Johnson Research Foundation colloquium, Philadelphia, April 1969. Academic Press, New York, 1971. Vol. 1, Probes and Membrane Function. Britton Chance, Chuan-Pu Lee, and J. Kent Blasie, Eds. xxx, 552 pp., illus. $13.50. Vol. 2, Probes of Enzymes and Hemoproteins. Britton Chance, Takashi Yonetani, and Albert

Kinetic evidence for Ca 2+ uptake by intact Ehrlich ascites tumor cells

FEBS LettersVolume 18, Issue 1 p. 98-102 Full-length articleFree Access Kinetic evidence for Ca2+ uptake by intact Ehrlich ascites tumor cells A. Cittadini, A. Cittadini Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pa. 19104, USA Present address: Istituto di Pathologia Generale, Università Cattolica Sacro Cuore, 00168 Roma, Italy Search for more papers by this authorA. Scarpa, A. Scarpa Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pa. 19104, USASearch for more papers by this authorB. Chance, B. Chance Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pa. 19104, USASearch for more papers by this author A. Cittadini, A. Cittadini Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pa. 19104, USA Present address: Istituto di Pathologia Generale, Università Cattolica Sacro Cuore, 00168 Roma, Italy Search for more papers by this authorA. Scarpa, A. Scarpa Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pa. 19104, USASearch for more papers by this authorB. Chance, B. Chance Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, Pa. 19104, USASearch for more papers by this author First published: October 15, 1971 https://doi.org/10.1016/0014-5793(71)80417-9Citations: 16 AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat References 1 J.F. Manery, C.L. Colmar F. Bronner Mineral Metabolism 3, (1969), Academic Press New York 405– 2 F.L. Bygrave, Nature, 214, (1967), 667– 3 D. Thomason, R. Schoeffield, Exptl. Cell Res., 16, (1959), 324– 4 F.L. Bygrave, Biochem. J., 101, (1966), 480– 5 C. Levinson, L.E. Blumenson, J. Cell Physiol., 75, (1970), 231– 6 T. Ohnishi, S. Ebashi, J. Biochem. (Tokyo), 54, (1963), 506– 7 F.F. Jobsis, M.G. O'Connor, Biochem. Biophys. Res. Commun., 25, (1966), 246– 8 L. Mela, B. Chance, Biochemistry, 7, (1968), 4059– 9 B. Chance, B. Hess, J. Biol. Chem., 234, (1959), 2404– 10 A. Scarpa, G.F. Azzone, J. Biol. Chem., 243, (1968), 5132– 11 B. Chance, Rev. Sci. Instr., 22, (1951), 634– 12 O. Dionisi, A. Cittadini, G. Gelmuzzi, T. Galeotti, T. Terranova, Biochim. Biophys. Acta, 216, (1970), 71– 13 B. Chance, P.K. Maitra, B. Wright Control Mechanisms in Respiration and Fermentation (1963), The Ronald Press New York 307– 14 B. Chance, J. Biol. Chem., 240, (1965), 2729– 15 A. Cittadini and A. Scarpa, manuscript in preparation. 16 L. Mela, Biochemistry, 8, (1969), 2481– 17 D. Schachter, S.M. Rosen, Am. J. Physiol., 196, (1959), 357– Citing Literature Volume18, Issue1October 15, 1971Pages 98-102 ReferencesRelatedInformation