Abstract:
:The dissociation of porcine erythrocyte catalase [EC 1.11.1.6] into subunits on denaturation with alkali, GuHCl and urea was investigated by following the changes in hydrodynamic properties, absorption and CD spectra in the Soret region and inactivation of the enzyme. It was found that dissociation proceeded in an "all or none" manner from the native tetramer (molecular weight, ca. 250,000) into identical 1/4-sized monomers (molecular weight, ca. 54,000 with alkali, 65,000 with urea and 71,000 with GuHCl) as estimated by ultracentrifugal analyses. On this dissociation, the sedimentation coefficient decreased from about 11S to 5.1 - 3.7S, and absorption spectra in the Soret region decreased to about 40% of the native level and showed a broad band around 365-375 nm and a shoulder around 415-420 nm; these changes were accompanied by complete loss of enzyme activity. The change in enzyme activity correlated well with that of absorption and CD spectra in the Soret region, depending on denaturation time, alkaline pH used and concentration of both denaturants. The reassociated catalase obtained by removing urea by dialysis was characterized by recovery of distinct CD bands in the Soret and near ultraviolet regions, although the partial refolding of alpha-helical conformation occurred without recovery of enzyme activity. These results indicate that the conformational changes and dissociation process of catalase into subunits can be monitored spectrophotometrically in relation to enzyme activity, and that subtle conformations near the heme groups and polypeptide backbone play an important role in maintaining full enzyme activity of the catalase molecule.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Takeda A,Hirano K,Shiroya Y,Samejima Tdoi
10.1093/oxfordjournals.jbchem.a134252subject
Has Abstractpub_date
1983-04-01 00:00:00pages
967-75issue
4eissn
0021-924Xissn
1756-2651journal_volume
93pub_type
杂志文章abstract::OsGEN-L has a 5'-flap endonuclease activity and plays an essential role in rice microspore development. The Class 4 RAD2/XPG family nucleases, including OsGEN-L, were recently found to have resolving activity for the Holliday junction (HJ), the intermediate of DNA strand recombination. In this study, we performed a de...
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doi:10.1093/oxfordjournals.jbchem.a132557
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journal_title:Journal of biochemistry
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1981-10-01 00:00:00
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pub_type: 杂志文章
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更新日期:1997-10-01 00:00:00
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pub_type: 杂志文章
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更新日期:1984-11-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a134682
更新日期:1984-03-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a022123
更新日期:1998-08-01 00:00:00
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journal_title:Journal of biochemistry
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更新日期:2010-02-01 00:00:00
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journal_title:Journal of biochemistry
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更新日期:2004-02-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章,评审
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更新日期:2013-02-01 00:00:00
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更新日期:2006-09-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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更新日期:1992-01-01 00:00:00
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journal_title:Journal of biochemistry
pub_type: 杂志文章
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更新日期:1985-05-01 00:00:00
abstract::In order to stabilize human RNase 1 by introduction of an intramolecular cross-link, a mutant protein (4-118CL RNase 1), in which Arg4 and Val118 are replaced with cysteine residues and linked by a disulfide bond, was designed and expressed in Escherichia coli as inclusion bodies. The 4-118CL RNase 1 that refolded und...
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journal_title:Journal of biochemistry
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更新日期:1982-02-01 00:00:00
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pub_type: 杂志文章
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更新日期:1998-04-01 00:00:00
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