Literature DB >> 4399047

IV. Cysteine proteinases. The structure of the papain molecule.

J Drenth, J N Jansonius, R Koekoek, L A Sluyterman, B G Wolthers.   

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Year:  1970        PMID： 4399047     DOI： 10.1098/rstb.1970.0022

Source DB:  PubMed          Journal:  Philos Trans R Soc Lond B Biol Sci        ISSN： 0962-8436            Impact factor:   6.237


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  6 in total

1.  A reinvestigation of residues 64-68 and 175 in papain. Evidence that residues 64 and 175 are asparagine.

Authors:  S S Husain; G Lowe
Journal:  Biochem J       Date:  1970-02       Impact factor: 3.857

Review 2.  Current problems in mechanistic studies of serine and cysteine proteinases.

Authors:  L Polgár; P Halász
Journal:  Biochem J       Date:  1982-10-01       Impact factor: 3.857

3.  Mass spectral characterization of organophosphate-labeled, tyrosine-containing peptides: characteristic mass fragments and a new binding motif for organophosphates.

Authors:  Lawrence M Schopfer; Hasmik Grigoryan; Bin Li; Florian Nachon; Patrick Masson; Oksana Lockridge
Journal:  J Chromatogr B Analyt Technol Biomed Life Sci       Date:  2009-07-24       Impact factor: 3.205

4.  Investigation of the active site of papain with fluorescent probes.

Authors:  G Allen; G Lowe
Journal:  Biochem J       Date:  1973-08       Impact factor: 3.857

5.  Chemically modified nylons as supports for enzyme immobilization. Polyisonitrile-nylon.

Authors:  L Goldstein; A Freeman; M Sokolovsky
Journal:  Biochem J       Date:  1974-12       Impact factor: 3.857

6.  Reactivities of the various protonic states in the reactions of papain and of L-cysteine with 2,2'- and with 4,4'- dipyridyl disulphide: evidence for nucleophilic reactivity in the un-ionized thiol group of the cysteine-25 residue of papain occasioned by its interaction with the histidine-159-asparagine-175 hydrogen-bonded system.

Authors:  K Brocklehurst; G Little
Journal:  Biochem J       Date:  1972-06       Impact factor: 3.857
  6 in total

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