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Article: Widespread occurrence of ganglioside-stimulated protein kinase in animal brains

TitleWidespread occurrence of ganglioside-stimulated protein kinase in animal brains
Authors
KeywordsCentral nervous system
Gangliosides
Protein kinases
Protein phosphorylation
Issue Date1997
PublisherS Karger AG. The Journal's web site is located at http://www.karger.com/NSG
Citation
Biological Signals, 1997, v. 6 n. 1, p. 21-28 How to Cite?
AbstractGanglioside-stimulated protein kinase, designated PKJ, had been found in several animal brains. These include guinea pig, rabbit, rat, and duck brains. All of the four brain PKJ could be extracted from the particulate fractions using nonionic detergent nonidet P-40 and purified by using identical DEAE-cellulose and phenyl-Sepharose chromatographic methods. These results suggest that PKJ from different animal brains has similar ionic and hydrophobic characteristics. All four of the partially purified PKJ preparations could undergo autophosphorylations in the presence of trisialoganglioside G(T1b) and 32P-ATP. Analyses of the autophosphorylated proteins by using SDS-polyacrylamide gel electrophoresis and subsequent autoradiography revealed one major radioactive band with apparent M(r) = 68,000. The range of ganglioside-stimulated autophosphorylation was between 6- and 10-fold. The structural similarities of the different animal brain PKJ were further determined by using one-dimensional peptide mapping techniques. Limited proteolytic cleavages of the 32P-labelled 68-kD bands with staphylococcal aureus V-8 protease resulted in four major radioactive fragments with apparent M(r) corresponding to 22, 20, 18 and 15-kD, respectively. By contrast, digestion with chymotrypsin revealed only two major radioactive bands with apparent M(r) of 43 and 26 kD, respectively. These findings indicate that PKJ from guinea pig, rabbit, rat, and duck brains may have similar primary structures.
Persistent Identifierhttp://hdl.handle.net/10722/68146
ISSN
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, KFJen_HK
dc.contributor.authorWai, SFen_HK
dc.date.accessioned2010-09-06T06:01:48Z-
dc.date.available2010-09-06T06:01:48Z-
dc.date.issued1997en_HK
dc.identifier.citationBiological Signals, 1997, v. 6 n. 1, p. 21-28en_HK
dc.identifier.issn1016-0922en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68146-
dc.description.abstractGanglioside-stimulated protein kinase, designated PKJ, had been found in several animal brains. These include guinea pig, rabbit, rat, and duck brains. All of the four brain PKJ could be extracted from the particulate fractions using nonionic detergent nonidet P-40 and purified by using identical DEAE-cellulose and phenyl-Sepharose chromatographic methods. These results suggest that PKJ from different animal brains has similar ionic and hydrophobic characteristics. All four of the partially purified PKJ preparations could undergo autophosphorylations in the presence of trisialoganglioside G(T1b) and 32P-ATP. Analyses of the autophosphorylated proteins by using SDS-polyacrylamide gel electrophoresis and subsequent autoradiography revealed one major radioactive band with apparent M(r) = 68,000. The range of ganglioside-stimulated autophosphorylation was between 6- and 10-fold. The structural similarities of the different animal brain PKJ were further determined by using one-dimensional peptide mapping techniques. Limited proteolytic cleavages of the 32P-labelled 68-kD bands with staphylococcal aureus V-8 protease resulted in four major radioactive fragments with apparent M(r) corresponding to 22, 20, 18 and 15-kD, respectively. By contrast, digestion with chymotrypsin revealed only two major radioactive bands with apparent M(r) of 43 and 26 kD, respectively. These findings indicate that PKJ from guinea pig, rabbit, rat, and duck brains may have similar primary structures.en_HK
dc.languageengen_HK
dc.publisherS Karger AG. The Journal's web site is located at http://www.karger.com/NSGen_HK
dc.relation.ispartofBiological Signalsen_HK
dc.rightsBiological Signals. Copyright © S Karger AG.en_HK
dc.subjectCentral nervous systemen_HK
dc.subjectGangliosidesen_HK
dc.subjectProtein kinasesen_HK
dc.subjectProtein phosphorylationen_HK
dc.titleWidespread occurrence of ganglioside-stimulated protein kinase in animal brainsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1016-0922&volume=6&spage=21&epage=28&date=1997&atitle=Widespread+occurrence+of+ganglioside-stimulated+protein+kinase+in+animal+brains.en_HK
dc.identifier.emailChan, KFJ: kfjchan@hkucc.hku.hken_HK
dc.identifier.authorityChan, KFJ=rp00378en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid9098520-
dc.identifier.scopuseid_2-s2.0-0030905151en_HK
dc.identifier.hkuros25336en_HK
dc.identifier.volume6en_HK
dc.identifier.issue1en_HK
dc.identifier.spage21en_HK
dc.identifier.epage28en_HK
dc.identifier.isiWOS:A1997WR09800003-
dc.publisher.placeSwitzerlanden_HK
dc.identifier.scopusauthoridChan, KFJ=7406035590en_HK
dc.identifier.scopusauthoridWai, SF=17037097000en_HK

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