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Journal Abstract Search

300 related items for PubMed ID: 11778

  • 1. 4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole as a reactivity probe for the investigation of the thiol proteinases. evidence that ficin and bromelain may lack carboxyl groups conformationally equivalent to that of aspartic acid-158 of papain.
    Shipton M, Stuchbury T, Brocklehurst K.
    Biochem J; 1976 Nov; 159(2):235-44. PubMed ID: 11778
    [Abstract] [Full Text] [Related]

  • 2. 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; 151(2):417-32. PubMed ID: 3168
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. Evaluation of benzofuroxan as a chromophoric oxidizing agent for thiol groups by using its reactions with papain, ficin, bromelain and low-molecular-weight thiols.
    Shipton M, Stuchbury T, Brocklehurst K.
    Biochem J; 1977 Mar 01; 161(3):627-37. PubMed ID: 851434
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. 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]

  • 7. 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
    [Abstract] [Full Text] [Related]

  • 8. 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]

  • 9. 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]

  • 10. Investigation of the active site of papain with fluorescent probes.
    Allen G, Lowe G.
    Biochem J; 1973 Aug 01; 133(4):679-86. PubMed ID: 4748829
    [Abstract] [Full Text] [Related]

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

  • 12. Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2'-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups.
    Baines BS, Brocklehurst K.
    Biochem J; 1982 Jul 01; 205(1):205-11. PubMed ID: 6751321
    [Abstract] [Full Text] [Related]

  • 13. 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]

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

  • 15. Differences between the electric fields of the catalytic sites of papain and actinidin detected by using the thiol-located nitrobenzofurazan label as a spectroscopic reporter group.
    Brocklehurst K, Salih E, Lodwig TS.
    Biochem J; 1984 Jun 01; 220(2):609-12. PubMed ID: 6378189
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. 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]

  • 18. 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]

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

  • 20. 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]

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