E. F. Hartree

Research Article| June 01 1951 Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin D. Keilin; D. Keilin 1Molteno Institute, University of Cambridge Search for other works by this author on: This Site PubMed Google Scholar E. F. Hartree E. F. Hartree 1Molteno Institute, University of Cambridge Search for other works by this author on: This Site PubMed Google Scholar Biochem J (1951) 49 (1): 88–106. https://doi.org/10.1042/bj0490088 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn Email Cite Icon Cite Get Permissions Citation D. Keilin, E. F. Hartree; Purification of horse-radish peroxidase and comparison of its properties with those of catalase and methaemoglobin. Biochem J 1 June 1951; 49 (1): 88–106. doi: https://doi.org/10.1042/bj0490088 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Journal Search Advanced Search © 1951 CAMBRIDGE UNIVERSITY PRESS1951 Article PDF first page preview Close Modal You do not currently have access to this content.

Research Article| January 01 1945 Properties of catalase. Catalysis of coupled oxidation of alcohols D. Keilin; D. Keilin 1The Molteno Institute, University of Cambridge Search for other works by this author on: This Site PubMed Google Scholar E. F. Hartree E. F. Hartree 1The Molteno Institute, University of Cambridge Search for other works by this author on: This Site PubMed Google Scholar Biochem J (1945) 39 (4): 293–301. https://doi.org/10.1042/bj0390293 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation D. Keilin, E. F. Hartree; Properties of catalase. Catalysis of coupled oxidation of alcohols. Biochem J 1 January 1945; 39 (4): 293–301. doi: https://doi.org/10.1042/bj0390293 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Journal Search Advanced Search This content is only available as a PDF. © 1945 CAMBRIDGE UNIVERSITY PRESS, ENGLAND1945 Article PDF first page preview Close Modal You do not currently have access to this content.

Abstract It was previously shown that the addition of cytochrome c to a heart-muscle preparation greatly increases its power of catalysing the oxidation of such substances as p-phenylene diamine, hydroquinone, cysteine and ascorbic acid. It was demonstrated that the oxidations of these substances, which can be used for the detection and estimation of intracellular oxidase, are catalysed not directly by the oxidase but through the co-operation of cytochrome. The only direct function of the oxidase, so far ascertained, is the oxidation of reduced cytochrome, and the enzyme can therefore be considered as cytochrome oxidase (Keilin and Hartree 1938a). Several properties which have been previously ascribed to it do not complete cytochrome-oxidase system. The object of this paper is the study of the mechanism of oxidation and reduction of cytochrome in order to determine the properties and the nature of cytochrome oxidase.

Abstract In a previous paper (Keilin and Hartree 1936) it was shown that catalase combines reversibly not only with KCN and H2S as was shown by Zeile and Hellstrom (1930) or with C2H5OOH (Stern 1936) but also with NaN3, NH2OH, N2H4, NaF and NO, giving corresponding spectroscopically well defined compounds. In this respect and in the general pattern of the absorption spectrum, catalase shows a striking resemblance to acid methaemoglobin. It differs, however, from the latter in three important properties, namely: