ISOLATION AND SEQUENCE DETERMINATION OF AN ACTIVE-SITE PEPTIDE OF RABBIT MUSCLE PYRUVATE-KINASE

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dc.contributor.authorBEZARES, G
dc.contributor.authorEYZAGUIRRE, J
dc.contributor.authorHINRICHS, MV
dc.contributor.authorHEINRIKSON, RL
dc.contributor.authorREARDON, I
dc.contributor.authorKEMP, RG
dc.contributor.authorLATSHAW, SP
dc.contributor.authorBAZAES, S
dc.date.accessioned2025-01-23T19:25:55Z
dc.date.available2025-01-23T19:25:55Z
dc.date.issued1987
dc.description.abstractRabbit muscle pyruvate kinase was inactivated by 2'',3''-dialdehyde ADP with the incorporation of one molecule of reagent per enzyme subunit. The inactivated protein was digested with trypsin after reduction and carboxymethylation. The labeled peptide was isolated by gel filtration and further purified by HPLC. The peptide was sequenced both by liquid-phase and gas-phase automatic Edman degradation. A 34-residue peptide was obtained. This peptide labeled with trinitrobenzenesulfonate, isolated and sequenced by Johnson et al. (Biochem. Biophys. Res. Commun. (1979) 90, 525-530) from bovine muscle pyruvate kinase. Available evidence suggests that dialdehyde ADP labels the enzyme at the same lysine in position 25 of the peptide, as found by Johnson et al. The high homology between the isolated peptide and regions of other pyruvate kinases from low to high eukaryotes supports the idea that this peptide is related to the enzyme active site.
dc.fuente.origenWOS
dc.identifier.eissn1096-0384
dc.identifier.issn0003-9861
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99542
dc.identifier.wosidWOS:A1987G002300015
dc.issue.numero1
dc.language.isoen
dc.pagina.final137
dc.pagina.inicio133
dc.revistaArchives of biochemistry and biophysics
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleISOLATION AND SEQUENCE DETERMINATION OF AN ACTIVE-SITE PEPTIDE OF RABBIT MUSCLE PYRUVATE-KINASE
dc.typeartículo
dc.volumen253
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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