These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

689 related items for PubMed ID: 3890831

  • 1. A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H.
    Willenbrock F, Brocklehurst K.
    Biochem J; 1985 Apr 15; 227(2):521-8. PubMed ID: 3890831
    [Abstract] [Full Text] [Related]

  • 2. 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
    [Abstract] [Full Text] [Related]

  • 3. 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
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5. 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]

  • 6. Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin.
    Knight CG.
    Biochem J; 1980 Sep 01; 189(3):447-53. PubMed ID: 7213339
    [Abstract] [Full Text] [Related]

  • 7. 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]

  • 8. 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]

  • 9. Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics.
    Brocklehurst K, Brocklehurst SM, Kowlessur D, O'Driscoll M, Patel G, Salih E, Templeton W, Thomas E, Topham CM, Willenbrock F.
    Biochem J; 1988 Dec 01; 256(2):543-58. PubMed ID: 3223929
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. 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]

  • 12. 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]

  • 13. Consequences of molecular recognition in the S1-S2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P1-P2 amide bond into a two-protonic-state reactivity probe.
    Brocklehurst K, Kowlessur D, Patel G, Templeton W, Quigley K, Thomas EW, Wharton CW, Willenbrock F, Szawelski RJ.
    Biochem J; 1988 Mar 15; 250(3):761-72. PubMed ID: 2839145
    [Abstract] [Full Text] [Related]

  • 14. Clarification of the pH-dependent kinetic behaviour of papain by using reactivity probes and analysis of alkylation and catalysed acylation reactions in terms of multihydronic state models: implications for electrostatics calculations and interpretation of the consequences of site-specific mutations such as Asp-158-Asn and Asp-158-Glu.
    Mellor GW, Patel M, Thomas EW, Brocklehurst K.
    Biochem J; 1993 Aug 15; 294 ( Pt 1)(Pt 1):201-10. PubMed ID: 8103322
    [Abstract] [Full Text] [Related]

  • 15. Sequence homologies, hydrophobic profiles and secondary structures of cathepsins B, H and L: comparison with papain and actinidin.
    Dufour E.
    Biochimie; 1988 Oct 15; 70(10):1335-42. PubMed ID: 3148320
    [Abstract] [Full Text] [Related]

  • 16. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors.
    Turk B, Turk V, Turk D.
    Biol Chem; 1997 Oct 15; 378(3-4):141-50. PubMed ID: 9165064
    [Abstract] [Full Text] [Related]

  • 17. Probing the specificity of cysteine proteinases at subsites remote from the active site: analysis of P4, P3, P2' and P3' variations in extended substrates.
    Portaro FC, Santos AB, Cezari MH, Juliano MA, Juliano L, Carmona E.
    Biochem J; 2000 Apr 01; 347 Pt 1(Pt 1):123-9. PubMed ID: 10727410
    [Abstract] [Full Text] [Related]

  • 18. The pH dependency of bovine spleen cathepsin B-catalyzed transfer of N alpha-benzyloxycarbonyl-L-lysine from p-nitrophenol to water and dipeptide nucleophiles. Comparisons with papain.
    Bajkowski AS, Frankfater A.
    J Biol Chem; 1983 Feb 10; 258(3):1650-5. PubMed ID: 6401725
    [Abstract] [Full Text] [Related]

  • 19. The role of Gly-4 of human cystatin A (stefin A) in the binding of target proteinases. Characterization by kinetic and equilibrium methods of the interactions of cystatin A Gly-4 mutants with papain, cathepsin B, and cathepsin L.
    Estrada S, Nycander M, Hill NJ, Craven CJ, Waltho JP, Björk I.
    Biochemistry; 1998 May 19; 37(20):7551-60. PubMed ID: 9585570
    [Abstract] [Full Text] [Related]

  • 20. Characterization by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases.
    Pol E, Olsson SL, Estrada S, Prasthofer TW, Björk I.
    Biochem J; 1995 Oct 01; 311 ( Pt 1)(Pt 1):275-82. PubMed ID: 7575465
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 35.