Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase
Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose. Reduced and denatured MDBH has a molecular weight of approximately 75,000. The unreduced MDBH has a molecular wei...
Gespeichert in:
| Veröffentlicht in: | Archives of biochemistry and biophysics 1981-10, Vol.211 (1), p.288-296 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 296 |
|---|---|
| container_issue | 1 |
| container_start_page | 288 |
| container_title | Archives of biochemistry and biophysics |
| container_volume | 211 |
| creator | Slater, Emily P. Zaremba, Samuel Hogue-Angeletti, Ruth A. |
| description | Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose. Reduced and denatured MDBH has a molecular weight of approximately 75,000. The unreduced MDBH has a molecular weight twice that size. MDBH and SDBH (soluble dopamine β-monooxygenase) possess many similar features. Using antiserum to SDBH, the two proteins show a reaction of identity in immunodiffusion assays. Their chromatographic, electrophoretic, and molecular weight characteristics are also very similar. Although the amino acid compositions of MDBH and SDBH were not dissimilar, the MDBH composition had a higher content of certain amino acids, particularly hydrophobic ones. Despite the remarkable likeness of MDBH and SDBH demonstrated above and by analytical peptide maps, peptides can be detected in MDBH which are not found in SDBH. |
| doi_str_mv | 10.1016/0003-9861(81)90456-2 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_73690967</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0003986181904562</els_id><sourcerecordid>15360443</sourcerecordid><originalsourceid>FETCH-LOGICAL-c388t-8caa43876855e173d912fc348380c299ccde73c3f7ddb74d0c67abc296ca58053</originalsourceid><addsrcrecordid>eNqFUc1qFTEUDqLU2583UMhK7GI0mWTy40KQ0lahUCm6DpnkpEZmJtdkpthdn6kP4jOZ23vpzro5Z_H9HM73IfSKkneUUPGeEMIarQR9q-ixJrwTTfsMrSjRoiFM8edo9Uh5ifZL-UkIpVy0e2hPSN1pLVbo7uuSY4jOzjFNOAU8wthnO0HTp2Xy2Ke1HeME-M99M6Yppd-31zDZAjjkNGL3o04bQpzwdVUtA5QP-AqGrd2ccEnD0g_wb59D9CLYocDRbh-g72en304-NxeX519OPl00jik1N8pZy5mSQnUdUMm8pm1wjCumiGu1ds6DZI4F6X0vuSdOSNtXRDjbKdKxA_Rm67vO6dcCZTZjLA6Gof6almIkE7omJ_9LpB0ThHNWiXxLdDmVkiGYdY6jzbeGErNpyGziN5v4jaLmoSHTVtnrnf_Sj-AfRbtKKv5xi0NN4yZCNsVFmBz4mMHNxqf49IG_mGmkKQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15360443</pqid></control><display><type>article</type><title>Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Slater, Emily P. ; Zaremba, Samuel ; Hogue-Angeletti, Ruth A.</creator><creatorcontrib>Slater, Emily P. ; Zaremba, Samuel ; Hogue-Angeletti, Ruth A.</creatorcontrib><description>Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose. Reduced and denatured MDBH has a molecular weight of approximately 75,000. The unreduced MDBH has a molecular weight twice that size. MDBH and SDBH (soluble dopamine β-monooxygenase) possess many similar features. Using antiserum to SDBH, the two proteins show a reaction of identity in immunodiffusion assays. Their chromatographic, electrophoretic, and molecular weight characteristics are also very similar. Although the amino acid compositions of MDBH and SDBH were not dissimilar, the MDBH composition had a higher content of certain amino acids, particularly hydrophobic ones. Despite the remarkable likeness of MDBH and SDBH demonstrated above and by analytical peptide maps, peptides can be detected in MDBH which are not found in SDBH.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(81)90456-2</identifier><identifier>PMID: 6795996</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adrenal Medulla - enzymology ; Amino Acid Sequence ; Animals ; cattle ; chromaffin granules ; Chromaffin Granules - enzymology ; Chromaffin System - enzymology ; dopamine beta -monooxygenase ; Dopamine beta-Hydroxylase - isolation & purification ; Dopamine beta-Hydroxylase - metabolism ; Immunodiffusion ; Intracellular Membranes - enzymology ; Isoenzymes - isolation & purification ; membranes ; Molecular Weight ; Peptide Fragments - analysis ; purification ; Solubility</subject><ispartof>Archives of biochemistry and biophysics, 1981-10, Vol.211 (1), p.288-296</ispartof><rights>1981</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-8caa43876855e173d912fc348380c299ccde73c3f7ddb74d0c67abc296ca58053</citedby><cites>FETCH-LOGICAL-c388t-8caa43876855e173d912fc348380c299ccde73c3f7ddb74d0c67abc296ca58053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986181904562$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6795996$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Slater, Emily P.</creatorcontrib><creatorcontrib>Zaremba, Samuel</creatorcontrib><creatorcontrib>Hogue-Angeletti, Ruth A.</creatorcontrib><title>Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose. Reduced and denatured MDBH has a molecular weight of approximately 75,000. The unreduced MDBH has a molecular weight twice that size. MDBH and SDBH (soluble dopamine β-monooxygenase) possess many similar features. Using antiserum to SDBH, the two proteins show a reaction of identity in immunodiffusion assays. Their chromatographic, electrophoretic, and molecular weight characteristics are also very similar. Although the amino acid compositions of MDBH and SDBH were not dissimilar, the MDBH composition had a higher content of certain amino acids, particularly hydrophobic ones. Despite the remarkable likeness of MDBH and SDBH demonstrated above and by analytical peptide maps, peptides can be detected in MDBH which are not found in SDBH.</description><subject>Adrenal Medulla - enzymology</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>cattle</subject><subject>chromaffin granules</subject><subject>Chromaffin Granules - enzymology</subject><subject>Chromaffin System - enzymology</subject><subject>dopamine beta -monooxygenase</subject><subject>Dopamine beta-Hydroxylase - isolation & purification</subject><subject>Dopamine beta-Hydroxylase - metabolism</subject><subject>Immunodiffusion</subject><subject>Intracellular Membranes - enzymology</subject><subject>Isoenzymes - isolation & purification</subject><subject>membranes</subject><subject>Molecular Weight</subject><subject>Peptide Fragments - analysis</subject><subject>purification</subject><subject>Solubility</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUc1qFTEUDqLU2583UMhK7GI0mWTy40KQ0lahUCm6DpnkpEZmJtdkpthdn6kP4jOZ23vpzro5Z_H9HM73IfSKkneUUPGeEMIarQR9q-ixJrwTTfsMrSjRoiFM8edo9Uh5ifZL-UkIpVy0e2hPSN1pLVbo7uuSY4jOzjFNOAU8wthnO0HTp2Xy2Ke1HeME-M99M6Yppd-31zDZAjjkNGL3o04bQpzwdVUtA5QP-AqGrd2ccEnD0g_wb59D9CLYocDRbh-g72en304-NxeX519OPl00jik1N8pZy5mSQnUdUMm8pm1wjCumiGu1ds6DZI4F6X0vuSdOSNtXRDjbKdKxA_Rm67vO6dcCZTZjLA6Gof6almIkE7omJ_9LpB0ThHNWiXxLdDmVkiGYdY6jzbeGErNpyGziN5v4jaLmoSHTVtnrnf_Sj-AfRbtKKv5xi0NN4yZCNsVFmBz4mMHNxqf49IG_mGmkKQ</recordid><startdate>19811001</startdate><enddate>19811001</enddate><creator>Slater, Emily P.</creator><creator>Zaremba, Samuel</creator><creator>Hogue-Angeletti, Ruth A.</creator><general>Elsevier Inc</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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19811001</creationdate><title>Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase</title><author>Slater, Emily P. ; Zaremba, Samuel ; Hogue-Angeletti, Ruth A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-8caa43876855e173d912fc348380c299ccde73c3f7ddb74d0c67abc296ca58053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Adrenal Medulla - enzymology</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>cattle</topic><topic>chromaffin granules</topic><topic>Chromaffin Granules - enzymology</topic><topic>Chromaffin System - enzymology</topic><topic>dopamine beta -monooxygenase</topic><topic>Dopamine beta-Hydroxylase - isolation & purification</topic><topic>Dopamine beta-Hydroxylase - metabolism</topic><topic>Immunodiffusion</topic><topic>Intracellular Membranes - enzymology</topic><topic>Isoenzymes - isolation & purification</topic><topic>membranes</topic><topic>Molecular Weight</topic><topic>Peptide Fragments - analysis</topic><topic>purification</topic><topic>Solubility</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Slater, Emily P.</creatorcontrib><creatorcontrib>Zaremba, Samuel</creatorcontrib><creatorcontrib>Hogue-Angeletti, Ruth A.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Slater, Emily P.</au><au>Zaremba, Samuel</au><au>Hogue-Angeletti, Ruth A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1981-10-01</date><risdate>1981</risdate><volume>211</volume><issue>1</issue><spage>288</spage><epage>296</epage><pages>288-296</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>Membrane-bound dopamine β-monooxygenase (MDBH) has been solubilized using emulphogen, a nonionic detergent, and purified by a single-step anion-exchange chromatography on DEAE-cellulose. Reduced and denatured MDBH has a molecular weight of approximately 75,000. The unreduced MDBH has a molecular weight twice that size. MDBH and SDBH (soluble dopamine β-monooxygenase) possess many similar features. Using antiserum to SDBH, the two proteins show a reaction of identity in immunodiffusion assays. Their chromatographic, electrophoretic, and molecular weight characteristics are also very similar. Although the amino acid compositions of MDBH and SDBH were not dissimilar, the MDBH composition had a higher content of certain amino acids, particularly hydrophobic ones. Despite the remarkable likeness of MDBH and SDBH demonstrated above and by analytical peptide maps, peptides can be detected in MDBH which are not found in SDBH.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6795996</pmid><doi>10.1016/0003-9861(81)90456-2</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Archives of biochemistry and biophysics, 1981-10, Vol.211 (1), p.288-296 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73690967 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Adrenal Medulla - enzymology Amino Acid Sequence Animals cattle chromaffin granules Chromaffin Granules - enzymology Chromaffin System - enzymology dopamine beta -monooxygenase Dopamine beta-Hydroxylase - isolation & purification Dopamine beta-Hydroxylase - metabolism Immunodiffusion Intracellular Membranes - enzymology Isoenzymes - isolation & purification membranes Molecular Weight Peptide Fragments - analysis purification Solubility |
| title | Purification of membrane-bound dopamine β-monooxygenase from chromaffin granules: Relation to soluble dopamine β-monooxygenase |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T19%3A12%3A55IST&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=Purification%20of%20membrane-bound%20dopamine%20%CE%B2-monooxygenase%20from%20chromaffin%20granules:%20Relation%20to%20soluble%20dopamine%20%CE%B2-monooxygenase&rft.jtitle=Archives%20of%20biochemistry%20and%20biophysics&rft.au=Slater,%20Emily%20P.&rft.date=1981-10-01&rft.volume=211&rft.issue=1&rft.spage=288&rft.epage=296&rft.pages=288-296&rft.issn=0003-9861&rft.eissn=1096-0384&rft_id=info:doi/10.1016/0003-9861(81)90456-2&rft_dat=%3Cproquest_cross%3E15360443%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=15360443&rft_id=info:pmid/6795996&rft_els_id=0003986181904562&rfr_iscdi=true |