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Journal Abstract Search


120 related items for PubMed ID: 687376

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  • 2. 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
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  • 3. 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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  • 5. A necessary modification to the preparation of papain from any high-quality latex of Carica papaya and evidence for the structural integrity of the enzyme produced by traditional methods.
    Baines BS, Brocklehurst K.
    Biochem J; 1979 Feb 01; 177(2):541-8. PubMed ID: 435250
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  • 6. 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
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  • 7. Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4.
    Willenbrock F, Brocklehurst K.
    Biochem J; 1985 Apr 15; 227(2):511-9. PubMed ID: 4004778
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  • 8. 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
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  • 9. 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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  • 16. 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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  • 18. 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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  • 19. 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
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  • 20. Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide).
    Willenbrock F, Brocklehurst K.
    Biochem J; 1984 Sep 15; 222(3):805-14. PubMed ID: 6534384
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