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166 related items for PubMed ID: 7006597
1. 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]
2. 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]
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 [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 [Abstract] [Full Text] [Related]
5. 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]
6. 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]
7. 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]
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]
12. 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]
13. 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 01; 159(2):235-44. PubMed ID: 11778 [Abstract] [Full Text] [Related]
14. A convenient method of preparation of high-activity urease from Canavalia ensiformis by covalent chromatography and an investigation of its thiol groups with 2,2'-dipyridyl disulphide as a thiol titrant and reactivity probe. Norris R, Brocklehurst K. Biochem J; 1976 Nov 01; 159(2):245-57. PubMed ID: 11779 [Abstract] [Full Text] [Related]
16. 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]
17. 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]
20. A spectrophotometric method for the detection of contaminant chymopapains in preparations of papain. Selective modification of one type of thiol group in the chymopapains by a two-protonic-state reagent. Baines BS, Brocklehurst K. Biochem J; 1978 Jul 01; 173(1):345-7. PubMed ID: 687376 [Abstract] [Full Text] [Related] Page: [Next] [New Search]