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379 related items for PubMed ID: 6347181

  • 1. A marked gradation in active-centre properties in the cysteine proteinases revealed by neutral and anionic reactivity probes. Reactivity characteristics of the thiol groups of actinidin, ficin, papain and papaya peptidase A towards 4,4'-dipyridyl disulphide and 5,5'-dithiobis-(2-nitrobenzoate) dianion.
    Brocklehurst K, Mushiri SM, Patel G, Willenbrock F.
    Biochem J; 1983 Mar 01; 209(3):873-9. PubMed ID: 6347181
    [Abstract] [Full Text] [Related]

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  • 3. Evidence that the active centre of chymopapain A is different from the active centres of some other cysteine proteinases and that the Brønsted coefficient (beta nuc.) for the reactions of thiolate anions with 2,2'-dipyridyl disulphide may be decreased by reagent protonation.
    Brocklehurst K, Baines BS, Mushiri MS.
    Biochem J; 1980 Jul 01; 189(1):189-29. PubMed ID: 7006597
    [Abstract] [Full Text] [Related]

  • 4. 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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  • 5. 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
    [Abstract] [Full Text] [Related]

  • 6. Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase omega. Three-dimensional structure of papaya proteinase omega deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis.
    Topham CM, Salih E, Frazao C, Kowlessur D, Overington JP, Thomas M, Brocklehurst SM, Patel M, Thomas EW, Brocklehurst K.
    Biochem J; 1991 Nov 15; 280 ( Pt 1)(Pt 1):79-92. PubMed ID: 1741760
    [Abstract] [Full Text] [Related]

  • 7. Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.
    Thomas MP, Topham CM, Kowlessur D, Mellor GW, Thomas EW, Whitford D, Brocklehurst K.
    Biochem J; 1994 Jun 15; 300 ( Pt 3)(Pt 3):805-20. PubMed ID: 8010964
    [Abstract] [Full Text] [Related]

  • 8. 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
    [Abstract] [Full Text] [Related]

  • 9. Reactions of papain and of low-molecular-weight thiols with some aromatic disulphides. 2,2'-Dipyridyl disulphide as a convenient active-site titrant for papain even in the presence of other thiols.
    Brocklehurst K, Little G.
    Biochem J; 1973 May 01; 133(1):67-80. PubMed ID: 4721623
    [Abstract] [Full Text] [Related]

  • 10. 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 01; 159(2):221-34. PubMed ID: 11777
    [Abstract] [Full Text] [Related]

  • 11. 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
    [Abstract] [Full Text] [Related]

  • 12. Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding.
    Brocklehurst K, Kowlessur D, O'Driscoll M, Patel G, Quenby S, Salih E, Templeton W, Thomas EW, Willenbrock F.
    Biochem J; 1987 May 15; 244(1):173-81. PubMed ID: 3663111
    [Abstract] [Full Text] [Related]

  • 13. Investigation of the catalytic site of actinidin by using benzofuroxan as a reactivity probe with selectivity for the thiolate-imidazolium ion-pair systems of cysteine proteinases. Evidence that the reaction of the ion-pair of actinidin (pKI 3.0, pKII 9.6) is modulated by the state of ionization of a group associated with a molecular pKa of 5.5.
    Salih E, Brocklehurst K.
    Biochem J; 1983 Sep 01; 213(3):713-8. PubMed ID: 6311173
    [Abstract] [Full Text] [Related]

  • 14. 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
    [Abstract] [Full Text] [Related]

  • 15. Characterization of the papain active centre by using two-protonic-state electrophiles as reactivity probes. Evidence for nucleophilic reactivity in the un-interrupted cysteine-25-histidine-159 interactive system.
    Shipton M, Brochlehurst K.
    Biochem J; 1978 May 01; 171(2):385-401. PubMed ID: 26335
    [Abstract] [Full Text] [Related]

  • 16. 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
    [Abstract] [Full Text] [Related]

  • 17. Variation in the P2-S2 stereochemical selectivity towards the enantiomeric N-acetylphenylalanylglycine 4-nitroanilides among the cysteine proteinases papain, ficin and actinidin.
    Patel M, Kayani IS, Mellor GW, Sreedharan S, Templeton W, Thomas EW, Thomas M, Brocklehurst K.
    Biochem J; 1992 Jan 15; 281 ( Pt 2)(Pt 2):553-9. PubMed ID: 1736903
    [Abstract] [Full Text] [Related]

  • 18. Mechanism of action of cysteine proteinases: oxyanion binding site is not essential in the hydrolysis of specific substrates.
    Asbóth B, Stokum E, Khan IU, Polgár L.
    Biochemistry; 1985 Jan 29; 24(3):606-9. PubMed ID: 3888259
    [Abstract] [Full Text] [Related]

  • 19. 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
    [Abstract] [Full Text] [Related]

  • 20. Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features.
    Gul S, Mellor GW, Thomas EW, Brocklehurst K.
    Biochem J; 2006 May 15; 396(1):17-21. PubMed ID: 16445383
    [Abstract] [Full Text] [Related]

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