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Journal Abstract Search

179 related items for PubMed ID: 23765

  • 1. Benzofuroxan as a thiol-specific reactivity probe. Kinetics of its reactions with papain, ficin, bromelain and low-molecular-weight thiols.
    Shipton M, Brocklehurst K.
    Biochem J; 1977 Dec 01; 167(3):799-810. PubMed ID: 23765
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  • 4. Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites.
    Willenbrock F, Brocklehurst K.
    Biochem J; 1986 Aug 15; 238(1):103-7. PubMed ID: 3800926
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  • 7. Reactivities of neutral and cationic forms of 2,2'-dipyridyl disulphide towards thiolate anions. Detection of differences between the active centres of actinidin, papain and ficin by a three-protonic-state reactivity probe.
    Brocklehurst K, Stuchbury T, Malthouse JP.
    Biochem J; 1979 Nov 01; 183(2):233-8. PubMed ID: 43130
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  • 8. Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin.
    Brocklehurst K, Malthouse JP.
    Biochem J; 1980 Dec 01; 191(3):707-18. PubMed ID: 7025834
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  • 9. A reporter group delivery system with both absolute and selective specificity for thiol groups and an improved fluorescent probe containing the 7-nitrobenzo-2-oxa-1,3-diazole moiety.
    Stuchbury T, Shipton M, Norris R, Malthouse JP, Brocklehurst K, Herbert JA, Suschitzky H.
    Biochem J; 1975 Nov 01; 151(2):417-32. PubMed ID: 3168
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  • 10. Evidence that binding to the s2-subsite of papain may be coupled with catalytically relevant structural change involving the cysteine-25-histidine-159 diad. Kinetics of the reaction of papain with a two-protonic-state reactivity probe containing a hydrophobic side chain.
    Brocklehurst K, Malthouse JP, Shipton M.
    Biochem J; 1979 Nov 01; 183(2):223-31. PubMed ID: 43129
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  • 12. Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.
    Salih E, Malthouse JP, Kowlessur D, Jarvis M, O'Driscoll M, Brocklehurst K.
    Biochem J; 1987 Oct 01; 247(1):181-93. PubMed ID: 2825655
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  • 15. Evidence for a close similarity in the catalytic sites of papain and ficin in near-neutral media despite differences in acidic and alkaline media. Kinetics of the reactions of papain and ficin with chloroacetate.
    Brocklehurst K, Mushiri SM, Patel G, Willenbrock F.
    Biochem J; 1982 Jan 01; 201(1):101-4. PubMed ID: 7044370
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  • 16. Comparison of the substrate conformations in the active sites of papain, chymopapain, ficin and bromelain by resonance Raman spectroscopy.
    Carey PR, Ozaki Y, Storer AC.
    Biochem Biophys Res Commun; 1983 Dec 28; 117(3):725-31. PubMed ID: 6365089
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  • 17. Preparation of fully active ficin from Ficus glabrata by covalent chromatography and characterization of its active centre by using 2,2'-depyridyl disulphide as a reactivity probe.
    Malthouse JP, Brocklehurst K.
    Biochem J; 1976 Nov 28; 159(2):221-34. PubMed ID: 11777
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  • 18. Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives.
    Baines BS, Brocklehurst K, Carey PR, Jarvis M, Salih E, Storer AC.
    Biochem J; 1986 Jan 01; 233(1):119-29. PubMed ID: 3513753
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  • 19. Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes.
    Brocklehurst K, Baines BS, Malthouse JP.
    Biochem J; 1981 Sep 01; 197(3):739-46. PubMed ID: 7034724
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  • 20. A kinetic method for the study of solvent environments of thiol groups in proteins involving the use of a pair of isomeric reactivity probes and a differential solvent effect. Investigation of the active centre of ficin by using 2,2'- and 4,4'- dipyridyl disulphides as reactivity probes.
    Malthouse JP, Brocklehurst K.
    Biochem J; 1980 Jan 01; 185(1):217-22. PubMed ID: 6990917
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