Partial purification and kinetic studies of mammalian tyrosinase
1. 1. The soluble tyrosinase used in this investigation was prepared from Harding-Passey mouse melanoma by the procedure of Brown and Ward with a slight modification. 2. 2. Electrophoretic analysis at pH 8.6 showed that this soluble tyrosinase contains two enzymically active components. 3. 3. Purifi...
Gespeichert in:
| Veröffentlicht in: | Biochimica et biophysica acta 1962-01, Vol.62 (2), p.205-215 |
|---|---|
| 1. Verfasser: | |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 215 |
|---|---|
| container_issue | 2 |
| container_start_page | 205 |
| container_title | Biochimica et biophysica acta |
| container_volume | 62 |
| creator | SHIMAO, K |
| description | 1.
1. The soluble tyrosinase used in this investigation was prepared from Harding-Passey mouse melanoma by the procedure of
Brown and Ward with a slight modification.
2.
2. Electrophoretic analysis at pH 8.6 showed that this soluble tyrosinase contains two enzymically active components.
3.
3. Purification of the preparation by salting-out with (NH
4)
2SO
4 did not make possible the complete separation of these two electrophoretically different components.
4.
4. The oxidation of DOPA into DOPA-quinone, as catalyzed by tyrosinase, was inhibited by tyrosine. Kinetic studies suggest that there are on the tyrosine molecule two kinds of sites: one where DOPA is oxidized and another where tyrosine is bound but not oxidized during the first phase of the reaction. |
| doi_str_mv | 10.1016/0006-3002(62)90034-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83060145</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0006300262900343</els_id><sourcerecordid>83060145</sourcerecordid><originalsourceid>FETCH-LOGICAL-c453t-34a9e1e940c9cc12d1106e1785c6574a11c69ae2a6e13dbf0fe6f4c7cc7774a3</originalsourceid><addsrcrecordid>eNp9kE1PwzAMhiMEgjH4Bwj1hOBQsJs0bS8INPElTYLD7lGWulKgHyNJkfbvydgEN0627Nd-7YexM4RrBJQ3ACBTDpBdyuyqAuAi5XtsgmVRppngYp9NfiVH7Nj795jkHKpDdoS8QqxENmF3b9oFq9tkNTrbWKODHfpE93XyYXsK1iQ-jLUlnwxN0umu063VfRLWbvC2155O2EGjW0-nuzhli8eHxew5nb8-vczu56kROQ8pF7oipEqAqYzBrEYESViUuZF5ITSikZWmTMcir5cNNCQbYQpjiiK2-ZRdbNeu3PA5kg-qs95Q2-qehtGrkoMEjFZTJrZCEy_0jhq1crbTbq0Q1Aac2lBRGypKZuoHnOJx7Hy3f1x2VP8N7UhFwe1WQPHJL0tOeWOpN1RbRyaoerD_O3wDhXF8nQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83060145</pqid></control><display><type>article</type><title>Partial purification and kinetic studies of mammalian tyrosinase</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>SHIMAO, K</creator><creatorcontrib>SHIMAO, K</creatorcontrib><description>1.
1. The soluble tyrosinase used in this investigation was prepared from Harding-Passey mouse melanoma by the procedure of
Brown and Ward with a slight modification.
2.
2. Electrophoretic analysis at pH 8.6 showed that this soluble tyrosinase contains two enzymically active components.
3.
3. Purification of the preparation by salting-out with (NH
4)
2SO
4 did not make possible the complete separation of these two electrophoretically different components.
4.
4. The oxidation of DOPA into DOPA-quinone, as catalyzed by tyrosinase, was inhibited by tyrosine. Kinetic studies suggest that there are on the tyrosine molecule two kinds of sites: one where DOPA is oxidized and another where tyrosine is bound but not oxidized during the first phase of the reaction.</description><identifier>ISSN: 0006-3002</identifier><identifier>EISSN: 1878-2434</identifier><identifier>DOI: 10.1016/0006-3002(62)90034-3</identifier><identifier>PMID: 13911942</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Animals ; Catechol Oxidase ; Kinetics ; Mammals ; Monophenol Monooxygenase ; Old Medline ; Oxidoreductases - chemistry</subject><ispartof>Biochimica et biophysica acta, 1962-01, Vol.62 (2), p.205-215</ispartof><rights>1962</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c453t-34a9e1e940c9cc12d1106e1785c6574a11c69ae2a6e13dbf0fe6f4c7cc7774a3</citedby><cites>FETCH-LOGICAL-c453t-34a9e1e940c9cc12d1106e1785c6574a11c69ae2a6e13dbf0fe6f4c7cc7774a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13911942$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>SHIMAO, K</creatorcontrib><title>Partial purification and kinetic studies of mammalian tyrosinase</title><title>Biochimica et biophysica acta</title><addtitle>Biochim Biophys Acta</addtitle><description>1.
1. The soluble tyrosinase used in this investigation was prepared from Harding-Passey mouse melanoma by the procedure of
Brown and Ward with a slight modification.
2.
2. Electrophoretic analysis at pH 8.6 showed that this soluble tyrosinase contains two enzymically active components.
3.
3. Purification of the preparation by salting-out with (NH
4)
2SO
4 did not make possible the complete separation of these two electrophoretically different components.
4.
4. The oxidation of DOPA into DOPA-quinone, as catalyzed by tyrosinase, was inhibited by tyrosine. Kinetic studies suggest that there are on the tyrosine molecule two kinds of sites: one where DOPA is oxidized and another where tyrosine is bound but not oxidized during the first phase of the reaction.</description><subject>Animals</subject><subject>Catechol Oxidase</subject><subject>Kinetics</subject><subject>Mammals</subject><subject>Monophenol Monooxygenase</subject><subject>Old Medline</subject><subject>Oxidoreductases - chemistry</subject><issn>0006-3002</issn><issn>1878-2434</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1962</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1PwzAMhiMEgjH4Bwj1hOBQsJs0bS8INPElTYLD7lGWulKgHyNJkfbvydgEN0627Nd-7YexM4RrBJQ3ACBTDpBdyuyqAuAi5XtsgmVRppngYp9NfiVH7Nj795jkHKpDdoS8QqxENmF3b9oFq9tkNTrbWKODHfpE93XyYXsK1iQ-jLUlnwxN0umu063VfRLWbvC2155O2EGjW0-nuzhli8eHxew5nb8-vczu56kROQ8pF7oipEqAqYzBrEYESViUuZF5ITSikZWmTMcir5cNNCQbYQpjiiK2-ZRdbNeu3PA5kg-qs95Q2-qehtGrkoMEjFZTJrZCEy_0jhq1crbTbq0Q1Aac2lBRGypKZuoHnOJx7Hy3f1x2VP8N7UhFwe1WQPHJL0tOeWOpN1RbRyaoerD_O3wDhXF8nQ</recordid><startdate>19620101</startdate><enddate>19620101</enddate><creator>SHIMAO, K</creator><general>Elsevier B.V</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>19620101</creationdate><title>Partial purification and kinetic studies of mammalian tyrosinase</title><author>SHIMAO, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c453t-34a9e1e940c9cc12d1106e1785c6574a11c69ae2a6e13dbf0fe6f4c7cc7774a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1962</creationdate><topic>Animals</topic><topic>Catechol Oxidase</topic><topic>Kinetics</topic><topic>Mammals</topic><topic>Monophenol Monooxygenase</topic><topic>Old Medline</topic><topic>Oxidoreductases - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>SHIMAO, K</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>Biochimica et biophysica acta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>SHIMAO, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Partial purification and kinetic studies of mammalian tyrosinase</atitle><jtitle>Biochimica et biophysica acta</jtitle><addtitle>Biochim Biophys Acta</addtitle><date>1962-01-01</date><risdate>1962</risdate><volume>62</volume><issue>2</issue><spage>205</spage><epage>215</epage><pages>205-215</pages><issn>0006-3002</issn><eissn>1878-2434</eissn><abstract>1.
1. The soluble tyrosinase used in this investigation was prepared from Harding-Passey mouse melanoma by the procedure of
Brown and Ward with a slight modification.
2.
2. Electrophoretic analysis at pH 8.6 showed that this soluble tyrosinase contains two enzymically active components.
3.
3. Purification of the preparation by salting-out with (NH
4)
2SO
4 did not make possible the complete separation of these two electrophoretically different components.
4.
4. The oxidation of DOPA into DOPA-quinone, as catalyzed by tyrosinase, was inhibited by tyrosine. Kinetic studies suggest that there are on the tyrosine molecule two kinds of sites: one where DOPA is oxidized and another where tyrosine is bound but not oxidized during the first phase of the reaction.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>13911942</pmid><doi>10.1016/0006-3002(62)90034-3</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-3002 |
| ispartof | Biochimica et biophysica acta, 1962-01, Vol.62 (2), p.205-215 |
| issn | 0006-3002 1878-2434 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_83060145 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Animals Catechol Oxidase Kinetics Mammals Monophenol Monooxygenase Old Medline Oxidoreductases - chemistry |
| title | Partial purification and kinetic studies of mammalian tyrosinase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T17%3A00%3A58IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Partial%20purification%20and%20kinetic%20studies%20of%20mammalian%20tyrosinase&rft.jtitle=Biochimica%20et%20biophysica%20acta&rft.au=SHIMAO,%20K&rft.date=1962-01-01&rft.volume=62&rft.issue=2&rft.spage=205&rft.epage=215&rft.pages=205-215&rft.issn=0006-3002&rft.eissn=1878-2434&rft_id=info:doi/10.1016/0006-3002(62)90034-3&rft_dat=%3Cproquest_cross%3E83060145%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=83060145&rft_id=info:pmid/13911942&rft_els_id=0006300262900343&rfr_iscdi=true |