Pig intestinal microvillar maltase-glucoamylase. Structure and membrane insertion
The NH2-terminal sequence (25 residues) of amphiphilic single polypeptide chain maltase-glucoamylase (EC 3.2.1.20) was determined by gas-phase sequencing. The result indicates that the NH2-terminal segment anchors the enzyme to the microvillar membrane. The single-chain form and the proteolytically...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 1986-09, Vol.261 (26), p.12306-12309 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 12309 |
|---|---|
| container_issue | 26 |
| container_start_page | 12306 |
| container_title | The Journal of biological chemistry |
| container_volume | 261 |
| creator | Norén, O Sjöström, H Cowell, G M Tranum-Jensen, J Hansen, O C Welinder, K G |
| description | The NH2-terminal sequence (25 residues) of amphiphilic single polypeptide chain maltase-glucoamylase (EC 3.2.1.20) was determined by gas-phase sequencing. The result indicates that the NH2-terminal segment anchors the enzyme to the microvillar membrane. The single-chain form and the proteolytically processed two-chain form have two distinct active sites differing in heat stability. However, both sites are sensitive to chonduritol B-epoxide and have similar substrate specificity. The amphiphilic single-chain maltase-glucoamylase and the amphiphilic proteolytically processed form were inserted into liposomes and studied by electron microscopy. The results showed that the enzyme is predominantly present as a homodimeric complex in the membrane. |
| doi_str_mv | 10.1016/S0021-9258(18)67239-4 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77004089</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925818672394</els_id><sourcerecordid>77004089</sourcerecordid><originalsourceid>FETCH-LOGICAL-c465t-677df12fa1522767d9d1614004abddc410ead1622ad26ad47eaccbf83002ebd73</originalsourceid><addsrcrecordid>eNqFkF-L1TAQxYMo63X1Iyz0QUQfumbSNmmfZFn8Bwsqq-BbmCbTeyNNuybtyn57Z_dero8GQkjmdyZnjhBnIM9Bgn57LaWCslNN-xraN9qoqivrR2IDsq3KqoGfj8XmiDwVz3L-JXnVHZyIk6pRLTTNRnz7GrZFmBbKS5hwLGJwab4N44ipiDgumKncjqubMd6NfDkvrpe0umVNVODki0ixTzgR98iUljBPz8WTAcdMLw7nqfjx4f33y0_l1ZePny8vrkpX62YptTF-ADUgNEoZbXznQUPNBrH33tUgCflFKfRKo68NoXP90FY8E_XeVKfi1b7vTZp_r-zfxpAdsfOJ5jVbY7iXbDsGmz3Ik-WcaLA3KURMdxakvY_SPkRp73Oy0NqHKG3NurPDB2sfyR9Vh-y4_vJQx-xwHDgGF_IRa6XpVAX_sF3Y7v6ERLYPs9tRtEoDbwuqkpqxd3uMOLPbQMlmF2hy5FniFuvn8B-_fwF2sZ0I</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77004089</pqid></control><display><type>article</type><title>Pig intestinal microvillar maltase-glucoamylase. Structure and membrane insertion</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Norén, O ; Sjöström, H ; Cowell, G M ; Tranum-Jensen, J ; Hansen, O C ; Welinder, K G</creator><creatorcontrib>Norén, O ; Sjöström, H ; Cowell, G M ; Tranum-Jensen, J ; Hansen, O C ; Welinder, K G</creatorcontrib><description>The NH2-terminal sequence (25 residues) of amphiphilic single polypeptide chain maltase-glucoamylase (EC 3.2.1.20) was determined by gas-phase sequencing. The result indicates that the NH2-terminal segment anchors the enzyme to the microvillar membrane. The single-chain form and the proteolytically processed two-chain form have two distinct active sites differing in heat stability. However, both sites are sensitive to chonduritol B-epoxide and have similar substrate specificity. The amphiphilic single-chain maltase-glucoamylase and the amphiphilic proteolytically processed form were inserted into liposomes and studied by electron microscopy. The results showed that the enzyme is predominantly present as a homodimeric complex in the membrane.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)67239-4</identifier><identifier>PMID: 3528155</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>alpha-Glucosidases - analysis ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Glucosidases - analysis ; Hydrolases ; Intestines - ultrastructure ; Liposomes ; Membrane Proteins - analysis ; Microscopy, Electron ; Microvilli - enzymology ; Models, Molecular ; Swine</subject><ispartof>The Journal of biological chemistry, 1986-09, Vol.261 (26), p.12306-12309</ispartof><rights>1986 © 1986 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c465t-677df12fa1522767d9d1614004abddc410ead1622ad26ad47eaccbf83002ebd73</citedby><cites>FETCH-LOGICAL-c465t-677df12fa1522767d9d1614004abddc410ead1622ad26ad47eaccbf83002ebd73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8079231$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3528155$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Norén, O</creatorcontrib><creatorcontrib>Sjöström, H</creatorcontrib><creatorcontrib>Cowell, G M</creatorcontrib><creatorcontrib>Tranum-Jensen, J</creatorcontrib><creatorcontrib>Hansen, O C</creatorcontrib><creatorcontrib>Welinder, K G</creatorcontrib><title>Pig intestinal microvillar maltase-glucoamylase. Structure and membrane insertion</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The NH2-terminal sequence (25 residues) of amphiphilic single polypeptide chain maltase-glucoamylase (EC 3.2.1.20) was determined by gas-phase sequencing. The result indicates that the NH2-terminal segment anchors the enzyme to the microvillar membrane. The single-chain form and the proteolytically processed two-chain form have two distinct active sites differing in heat stability. However, both sites are sensitive to chonduritol B-epoxide and have similar substrate specificity. The amphiphilic single-chain maltase-glucoamylase and the amphiphilic proteolytically processed form were inserted into liposomes and studied by electron microscopy. The results showed that the enzyme is predominantly present as a homodimeric complex in the membrane.</description><subject>alpha-Glucosidases - analysis</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucosidases - analysis</subject><subject>Hydrolases</subject><subject>Intestines - ultrastructure</subject><subject>Liposomes</subject><subject>Membrane Proteins - analysis</subject><subject>Microscopy, Electron</subject><subject>Microvilli - enzymology</subject><subject>Models, Molecular</subject><subject>Swine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkF-L1TAQxYMo63X1Iyz0QUQfumbSNmmfZFn8Bwsqq-BbmCbTeyNNuybtyn57Z_dero8GQkjmdyZnjhBnIM9Bgn57LaWCslNN-xraN9qoqivrR2IDsq3KqoGfj8XmiDwVz3L-JXnVHZyIk6pRLTTNRnz7GrZFmBbKS5hwLGJwab4N44ipiDgumKncjqubMd6NfDkvrpe0umVNVODki0ixTzgR98iUljBPz8WTAcdMLw7nqfjx4f33y0_l1ZePny8vrkpX62YptTF-ADUgNEoZbXznQUPNBrH33tUgCflFKfRKo68NoXP90FY8E_XeVKfi1b7vTZp_r-zfxpAdsfOJ5jVbY7iXbDsGmz3Ik-WcaLA3KURMdxakvY_SPkRp73Oy0NqHKG3NurPDB2sfyR9Vh-y4_vJQx-xwHDgGF_IRa6XpVAX_sF3Y7v6ERLYPs9tRtEoDbwuqkpqxd3uMOLPbQMlmF2hy5FniFuvn8B-_fwF2sZ0I</recordid><startdate>19860915</startdate><enddate>19860915</enddate><creator>Norén, O</creator><creator>Sjöström, H</creator><creator>Cowell, G M</creator><creator>Tranum-Jensen, J</creator><creator>Hansen, O C</creator><creator>Welinder, K G</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><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>19860915</creationdate><title>Pig intestinal microvillar maltase-glucoamylase. Structure and membrane insertion</title><author>Norén, O ; Sjöström, H ; Cowell, G M ; Tranum-Jensen, J ; Hansen, O C ; Welinder, K G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c465t-677df12fa1522767d9d1614004abddc410ead1622ad26ad47eaccbf83002ebd73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>alpha-Glucosidases - analysis</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucosidases - analysis</topic><topic>Hydrolases</topic><topic>Intestines - ultrastructure</topic><topic>Liposomes</topic><topic>Membrane Proteins - analysis</topic><topic>Microscopy, Electron</topic><topic>Microvilli - enzymology</topic><topic>Models, Molecular</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Norén, O</creatorcontrib><creatorcontrib>Sjöström, H</creatorcontrib><creatorcontrib>Cowell, G M</creatorcontrib><creatorcontrib>Tranum-Jensen, J</creatorcontrib><creatorcontrib>Hansen, O C</creatorcontrib><creatorcontrib>Welinder, K G</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><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>Norén, O</au><au>Sjöström, H</au><au>Cowell, G M</au><au>Tranum-Jensen, J</au><au>Hansen, O C</au><au>Welinder, K G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Pig intestinal microvillar maltase-glucoamylase. Structure and membrane insertion</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1986-09-15</date><risdate>1986</risdate><volume>261</volume><issue>26</issue><spage>12306</spage><epage>12309</epage><pages>12306-12309</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>The NH2-terminal sequence (25 residues) of amphiphilic single polypeptide chain maltase-glucoamylase (EC 3.2.1.20) was determined by gas-phase sequencing. The result indicates that the NH2-terminal segment anchors the enzyme to the microvillar membrane. The single-chain form and the proteolytically processed two-chain form have two distinct active sites differing in heat stability. However, both sites are sensitive to chonduritol B-epoxide and have similar substrate specificity. The amphiphilic single-chain maltase-glucoamylase and the amphiphilic proteolytically processed form were inserted into liposomes and studied by electron microscopy. The results showed that the enzyme is predominantly present as a homodimeric complex in the membrane.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3528155</pmid><doi>10.1016/S0021-9258(18)67239-4</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1986-09, Vol.261 (26), p.12306-12309 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77004089 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | alpha-Glucosidases - analysis Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glucosidases - analysis Hydrolases Intestines - ultrastructure Liposomes Membrane Proteins - analysis Microscopy, Electron Microvilli - enzymology Models, Molecular Swine |
| title | Pig intestinal microvillar maltase-glucoamylase. Structure and membrane insertion |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-22T04%3A23%3A02IST&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=Pig%20intestinal%20microvillar%20maltase-glucoamylase.%20Structure%20and%20membrane%20insertion&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Nor%C3%A9n,%20O&rft.date=1986-09-15&rft.volume=261&rft.issue=26&rft.spage=12306&rft.epage=12309&rft.pages=12306-12309&rft.issn=0021-9258&rft.eissn=1083-351X&rft.coden=JBCHA3&rft_id=info:doi/10.1016/S0021-9258(18)67239-4&rft_dat=%3Cproquest_cross%3E77004089%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=77004089&rft_id=info:pmid/3528155&rft_els_id=S0021925818672394&rfr_iscdi=true |