Purification and Properties of the Catalase of Bakers' Yeast
Catalase from bakers' yeast has been purified to homogeneity in the analytical ultracentrifuge and in gel electrophoresis; sedimentation measurements permit an estimation of its molecular weight as 248,000. Under denaturing conditions, polyacrylamide gel electrophoresis revealed dissociation of...
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| Veröffentlicht in: | The Journal of biological chemistry 1973-04, Vol.248 (8), p.2889-2893 |
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| container_title | The Journal of biological chemistry |
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| creator | Seah, T C Kaplan, J G |
| description | Catalase from bakers' yeast has been purified to homogeneity in the analytical ultracentrifuge and in gel electrophoresis;
sedimentation measurements permit an estimation of its molecular weight as 248,000. Under denaturing conditions, polyacrylamide
gel electrophoresis revealed dissociation of a major component of molecular weight 61,000, which constituted 90% of the total
protein of the stained gel, suggesting that the native enzyme is tetrameric. The iron content was 0.096%, corresponding to
a subunit molecular weight of 58,000. Specific activity was high (Kat. f. = 66,000); catalytic and spectroscopic properties
were similar to those of catalases from other species. The enzyme is present in commercial yeast and in a variety of haploid
and diploid wild type strains. |
| doi_str_mv | 10.1016/s0021-9258(19)44090-8 |
| format | Article |
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sedimentation measurements permit an estimation of its molecular weight as 248,000. Under denaturing conditions, polyacrylamide
gel electrophoresis revealed dissociation of a major component of molecular weight 61,000, which constituted 90% of the total
protein of the stained gel, suggesting that the native enzyme is tetrameric. The iron content was 0.096%, corresponding to
a subunit molecular weight of 58,000. Specific activity was high (Kat. f. = 66,000); catalytic and spectroscopic properties
were similar to those of catalases from other species. The enzyme is present in commercial yeast and in a variety of haploid
and diploid wild type strains.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/s0021-9258(19)44090-8</identifier><identifier>PMID: 4572513</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Catalase - analysis ; Catalase - isolation & purification ; Catalase - metabolism ; Centrifugation, Density Gradient ; Chromatography ; Chromatography, Gel ; Diploidy ; Electrophoresis, Polyacrylamide Gel ; Haploidy ; Hydrogen-Ion Concentration ; Iron - analysis ; Kinetics ; Molecular Weight ; Saccharomyces cerevisiae - enzymology ; Spectrophotometry</subject><ispartof>The Journal of biological chemistry, 1973-04, Vol.248 (8), p.2889-2893</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c444t-fbf18a2031589e098bab3740dc3ac96e1f47d54d3bddced7763d86b51aa7c90c3</citedby><cites>FETCH-LOGICAL-c444t-fbf18a2031589e098bab3740dc3ac96e1f47d54d3bddced7763d86b51aa7c90c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4572513$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Seah, T C</creatorcontrib><creatorcontrib>Kaplan, J G</creatorcontrib><title>Purification and Properties of the Catalase of Bakers' Yeast</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Catalase from bakers' yeast has been purified to homogeneity in the analytical ultracentrifuge and in gel electrophoresis;
sedimentation measurements permit an estimation of its molecular weight as 248,000. Under denaturing conditions, polyacrylamide
gel electrophoresis revealed dissociation of a major component of molecular weight 61,000, which constituted 90% of the total
protein of the stained gel, suggesting that the native enzyme is tetrameric. The iron content was 0.096%, corresponding to
a subunit molecular weight of 58,000. Specific activity was high (Kat. f. = 66,000); catalytic and spectroscopic properties
were similar to those of catalases from other species. The enzyme is present in commercial yeast and in a variety of haploid
and diploid wild type strains.</description><subject>Catalase - analysis</subject><subject>Catalase - isolation & purification</subject><subject>Catalase - metabolism</subject><subject>Centrifugation, Density Gradient</subject><subject>Chromatography</subject><subject>Chromatography, Gel</subject><subject>Diploidy</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Haploidy</subject><subject>Hydrogen-Ion Concentration</subject><subject>Iron - analysis</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Spectrophotometry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1973</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kN1LwzAUxYMoc07_hEHxwY-HatIkbQK-6PALBg5U0KeQJrc22q4zaRH_e1s3dl8ul3POPfBDaErwBcEkvQwYJySWCRdnRJ4zhiWOxQ4aEyxoTDl520XjrWUfHYTwifthkozQiPEs4YSO0dWi865wRreuWUZ6aaOFb1bgWwchaoqoLSGa6VZXOsBw3-gv8OE0egcd2kO0V-gqwNFmT9Dr3e3L7CGeP90_zq7nsWGMtXGRF0ToBFPChQQsRa5zmjFsDdVGpkAKllnOLM2tNWCzLKVWpDknWmdGYkMn6GT9d-Wb7w5Cq2oXDFSVXkLTBSWIEDjJkt7I10bjmxA8FGrlXa39ryJYDdTU84BEDUgUkeqfmhJ9brop6PIa7Da1wdTrx2u9dB_lj_OgcteYEmqVMKGESoSQ9A84cnL7</recordid><startdate>19730425</startdate><enddate>19730425</enddate><creator>Seah, T C</creator><creator>Kaplan, J G</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19730425</creationdate><title>Purification and Properties of the Catalase of Bakers' Yeast</title><author>Seah, T C ; Kaplan, J G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c444t-fbf18a2031589e098bab3740dc3ac96e1f47d54d3bddced7763d86b51aa7c90c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1973</creationdate><topic>Catalase - analysis</topic><topic>Catalase - isolation & purification</topic><topic>Catalase - metabolism</topic><topic>Centrifugation, Density Gradient</topic><topic>Chromatography</topic><topic>Chromatography, Gel</topic><topic>Diploidy</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Haploidy</topic><topic>Hydrogen-Ion Concentration</topic><topic>Iron - analysis</topic><topic>Kinetics</topic><topic>Molecular Weight</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Seah, T C</creatorcontrib><creatorcontrib>Kaplan, J G</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Seah, T C</au><au>Kaplan, J G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Properties of the Catalase of Bakers' Yeast</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1973-04-25</date><risdate>1973</risdate><volume>248</volume><issue>8</issue><spage>2889</spage><epage>2893</epage><pages>2889-2893</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Catalase from bakers' yeast has been purified to homogeneity in the analytical ultracentrifuge and in gel electrophoresis;
sedimentation measurements permit an estimation of its molecular weight as 248,000. Under denaturing conditions, polyacrylamide
gel electrophoresis revealed dissociation of a major component of molecular weight 61,000, which constituted 90% of the total
protein of the stained gel, suggesting that the native enzyme is tetrameric. The iron content was 0.096%, corresponding to
a subunit molecular weight of 58,000. Specific activity was high (Kat. f. = 66,000); catalytic and spectroscopic properties
were similar to those of catalases from other species. The enzyme is present in commercial yeast and in a variety of haploid
and diploid wild type strains.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>4572513</pmid><doi>10.1016/s0021-9258(19)44090-8</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1973-04, Vol.248 (8), p.2889-2893 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81880272 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Catalase - analysis Catalase - isolation & purification Catalase - metabolism Centrifugation, Density Gradient Chromatography Chromatography, Gel Diploidy Electrophoresis, Polyacrylamide Gel Haploidy Hydrogen-Ion Concentration Iron - analysis Kinetics Molecular Weight Saccharomyces cerevisiae - enzymology Spectrophotometry |
| title | Purification and Properties of the Catalase of Bakers' Yeast |
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