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Article: Activity of the reduced zymogen of streptococcal proteinase.

TitleActivity of the reduced zymogen of streptococcal proteinase.
Authors
Issue Date1970
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 1970, v. 245 n. 4, p. 846-849 How to Cite?
AbstractReduction of the protein—S—S—R bond in the zymogen of streptococcal proteinase leads to an enzymatically active molecule without any proteolysis being required. This conclusion is based upon experiments in which the zymogen has been reduced in very dilute solution where the rate of bimolecular autodigestion is at a minimum. Under these conditions, even in the presence of 3.5 M guanidinium chloride, the rate of activation depends upon the concentration of reducing agent and does not depend upon the protein concentration; also, the amino acid composition of the activated zymogen is indistinguishable from that of the starting material. In the more concentrated solutions that have usually been employed for autodigestion, reduced zymogen molecules can initiate the autodigestion that leads to removal of about 100 amino acid residues. The end product in that case has been shown earlier to be similar to that obtained when the conversion is accomplished by controlled proteolysis with trypsin followed by reduction of the protein—S—S—R bond. In aqueous solution, the rate of reduction of the disulfide bond in the zymogen is slow relative to the rate of its reduction in the molecule obtained after proteolysis. The slowness of reduction contributes to the stability of the zymogen in dilute solutions under mildly reducing conditions such as may exist in bacterial cultures in the early stages of growth. The rate of reduction can be accelerated in vitro by the partial unfolding of the molecule induced by the addition of guanidinium chloride. The reduced zymogen and the reduced proteolyzed zymogen possess similar specific activities. The nature of the zymogen-enzyme relationship for this enzyme of bacterial origin differs from that which has been established for the zymogens of pancreatic proteinases where proteolysis is a prerequisite for activity.
Persistent Identifierhttp://hdl.handle.net/10722/167420
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBustin, Men_US
dc.contributor.authorLin, MCen_US
dc.contributor.authorStein, WHen_US
dc.contributor.authorMoore, Sen_US
dc.date.accessioned2012-10-08T03:06:44Z-
dc.date.available2012-10-08T03:06:44Z-
dc.date.issued1970en_US
dc.identifier.citationJournal Of Biological Chemistry, 1970, v. 245 n. 4, p. 846-849en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/167420-
dc.description.abstractReduction of the protein—S—S—R bond in the zymogen of streptococcal proteinase leads to an enzymatically active molecule without any proteolysis being required. This conclusion is based upon experiments in which the zymogen has been reduced in very dilute solution where the rate of bimolecular autodigestion is at a minimum. Under these conditions, even in the presence of 3.5 M guanidinium chloride, the rate of activation depends upon the concentration of reducing agent and does not depend upon the protein concentration; also, the amino acid composition of the activated zymogen is indistinguishable from that of the starting material. In the more concentrated solutions that have usually been employed for autodigestion, reduced zymogen molecules can initiate the autodigestion that leads to removal of about 100 amino acid residues. The end product in that case has been shown earlier to be similar to that obtained when the conversion is accomplished by controlled proteolysis with trypsin followed by reduction of the protein—S—S—R bond. In aqueous solution, the rate of reduction of the disulfide bond in the zymogen is slow relative to the rate of its reduction in the molecule obtained after proteolysis. The slowness of reduction contributes to the stability of the zymogen in dilute solutions under mildly reducing conditions such as may exist in bacterial cultures in the early stages of growth. The rate of reduction can be accelerated in vitro by the partial unfolding of the molecule induced by the addition of guanidinium chloride. The reduced zymogen and the reduced proteolyzed zymogen possess similar specific activities. The nature of the zymogen-enzyme relationship for this enzyme of bacterial origin differs from that which has been established for the zymogens of pancreatic proteinases where proteolysis is a prerequisite for activity.-
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.subject.meshAmino Acids - Analysisen_US
dc.subject.meshBiochemical Phenomenaen_US
dc.subject.meshBiochemistryen_US
dc.subject.meshChromatography, Gelen_US
dc.subject.meshEndopeptidases - Analysisen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshEnzyme Precursorsen_US
dc.subject.meshEsterasesen_US
dc.subject.meshGuanidinesen_US
dc.subject.meshKineticsen_US
dc.subject.meshMercaptoethanolen_US
dc.subject.meshOxidation-Reductionen_US
dc.subject.meshPancreas - Enzymologyen_US
dc.subject.meshSpecies Specificityen_US
dc.subject.meshSpectrophotometryen_US
dc.subject.meshStreptococcus - Enzymologyen_US
dc.subject.meshSulfidesen_US
dc.subject.meshTrypsinen_US
dc.subject.meshUltraviolet Raysen_US
dc.subject.meshUreaen_US
dc.titleActivity of the reduced zymogen of streptococcal proteinase.en_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.pmid5416667-
dc.identifier.scopuseid_2-s2.0-0014961396en_US
dc.identifier.volume245en_US
dc.identifier.issue4en_US
dc.identifier.spage846en_US
dc.identifier.epage849en_US
dc.identifier.isiWOS:A1970F563900028-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBustin, M=7101676820en_US
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridStein, WH=7201784892en_US
dc.identifier.scopusauthoridMoore, S=7403537387en_US

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