Dissociation of Bovine 6S Procarboxypeptidase A by Reversible Condensation with 2,3-dimethyl Maleic Anhydride: Application to the Partial Characterization of Subunit III
Bovine 6S procarboxypeptidase A can be dissociated into its three subunits by acylation with dimethyl maleic anhydride. The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1975-06, Vol.72 (6), p.2442-2445 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Puigserver, A. Desnuelle, P. |
| description | Bovine 6S procarboxypeptidase A can be dissociated into its three subunits by acylation with dimethyl maleic anhydride. The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same residues in bovine chymotrypsinogen A and C (subunit II) and also in proelastase A of the African lungfish. Therefore, this subunit is likely to be a chymotrypsinogen or proelastase-A-like zymogen which has lost the ability to be activated on account of a deletion of the N-terminal residues from half-cystine 1 to valine 17. Like other pancreatic zymogens, subunit III appears to possess a weakly functional active site. |
| doi_str_mv | 10.1073/pnas.72.6.2442 |
| format | Article |
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The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same residues in bovine chymotrypsinogen A and C (subunit II) and also in proelastase A of the African lungfish. Therefore, this subunit is likely to be a chymotrypsinogen or proelastase-A-like zymogen which has lost the ability to be activated on account of a deletion of the N-terminal residues from half-cystine 1 to valine 17. Like other pancreatic zymogens, subunit III appears to possess a weakly functional active site.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.72.6.2442</identifier><identifier>PMID: 237272</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Active sites ; Acylation ; Amino Acid Sequence ; Amino Acids - analysis ; Anhydrides ; Animals ; Biochemistry ; Carboxypeptidases - analysis ; Cattle ; Chemical Phenomena ; Chemistry ; Chromatography, DEAE-Cellulose ; Chromatography, Gel ; Condensation ; Endopeptidases ; Enzyme Precursors - analysis ; Hydrogen-Ion Concentration ; Macromolecular Substances ; Maleates ; Pancreas ; Pancreas - enzymology ; Peptides - analysis ; Peptides - isolation & purification ; Proteins ; Trimers ; Ungulates ; Zymogens</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1975-06, Vol.72 (6), p.2442-2445</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3702-12ab6921904657715f9c9e100218362592417ea6889142f8e28cba8f5f93d4c83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/72/6.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/64727$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/64727$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/237272$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Puigserver, A.</creatorcontrib><creatorcontrib>Desnuelle, P.</creatorcontrib><title>Dissociation of Bovine 6S Procarboxypeptidase A by Reversible Condensation with 2,3-dimethyl Maleic Anhydride: Application to the Partial Characterization of Subunit III</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Bovine 6S procarboxypeptidase A can be dissociated into its three subunits by acylation with dimethyl maleic anhydride. The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same residues in bovine chymotrypsinogen A and C (subunit II) and also in proelastase A of the African lungfish. Therefore, this subunit is likely to be a chymotrypsinogen or proelastase-A-like zymogen which has lost the ability to be activated on account of a deletion of the N-terminal residues from half-cystine 1 to valine 17. Like other pancreatic zymogens, subunit III appears to possess a weakly functional active site.</description><subject>Active sites</subject><subject>Acylation</subject><subject>Amino Acid Sequence</subject><subject>Amino Acids - analysis</subject><subject>Anhydrides</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Carboxypeptidases - analysis</subject><subject>Cattle</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Chromatography, Gel</subject><subject>Condensation</subject><subject>Endopeptidases</subject><subject>Enzyme Precursors - analysis</subject><subject>Hydrogen-Ion Concentration</subject><subject>Macromolecular Substances</subject><subject>Maleates</subject><subject>Pancreas</subject><subject>Pancreas - enzymology</subject><subject>Peptides - analysis</subject><subject>Peptides - isolation & purification</subject><subject>Proteins</subject><subject>Trimers</subject><subject>Ungulates</subject><subject>Zymogens</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc1u1DAUhSPE31DYskAgecWKDLbjsR0kFtPhb6QiKgpry3FuiCtPHGxn2vBGvCUZpYzKhpUX5_t8r-7JsqcELwkWxeu-03Ep6JIvKWP0TrYguCQ5ZyW-my0wpiKXjLKH2aMYLzHG5UriB9l9Wggq6CL7_c7G6I3VyfoO-Qad-r3tAPELdB680aHy12MPfbK1joDWqBrRV9hDiLZygDa-q6GLs31lU4voqyKv7Q5SOzr0WTuwBq27dqyDreENWve9s2bmk0epBXSuQ7LaoU2rgzYJgv113OZiqIbOJrTdbh9n9xrtIjy5eU-y7x_ef9t8ys--fNxu1me5KQSmOaG64iUlJWZ8JQRZNaUpgUyHILLgdFVSRgRoLmVJGG0kUGkqLZuJK2pmZHGSvZ3_7YdqB7WBLgXtVB_sTodReW3Vv0lnW_XD7xUrqBCryX954wf_c4CY1M5GA87pDvwQlaSSC8zJBC5n0AQfY4DmOINgdahWHapVgiquDtVOwvPbmx3xuctbgw_a3_Coq2ZwLsF1msAX_wOn_NmcX8bkwxHgbBpT_AHiZ8Jw</recordid><startdate>19750601</startdate><enddate>19750601</enddate><creator>Puigserver, A.</creator><creator>Desnuelle, P.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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><scope>5PM</scope></search><sort><creationdate>19750601</creationdate><title>Dissociation of Bovine 6S Procarboxypeptidase A by Reversible Condensation with 2,3-dimethyl Maleic Anhydride: Application to the Partial Characterization of Subunit III</title><author>Puigserver, A. ; Desnuelle, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3702-12ab6921904657715f9c9e100218362592417ea6889142f8e28cba8f5f93d4c83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Active sites</topic><topic>Acylation</topic><topic>Amino Acid Sequence</topic><topic>Amino Acids - analysis</topic><topic>Anhydrides</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Carboxypeptidases - analysis</topic><topic>Cattle</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Chromatography, Gel</topic><topic>Condensation</topic><topic>Endopeptidases</topic><topic>Enzyme Precursors - analysis</topic><topic>Hydrogen-Ion Concentration</topic><topic>Macromolecular Substances</topic><topic>Maleates</topic><topic>Pancreas</topic><topic>Pancreas - enzymology</topic><topic>Peptides - analysis</topic><topic>Peptides - isolation & purification</topic><topic>Proteins</topic><topic>Trimers</topic><topic>Ungulates</topic><topic>Zymogens</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Puigserver, A.</creatorcontrib><creatorcontrib>Desnuelle, P.</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Puigserver, A.</au><au>Desnuelle, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Dissociation of Bovine 6S Procarboxypeptidase A by Reversible Condensation with 2,3-dimethyl Maleic Anhydride: Application to the Partial Characterization of Subunit III</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1975-06-01</date><risdate>1975</risdate><volume>72</volume><issue>6</issue><spage>2442</spage><epage>2445</epage><pages>2442-2445</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Bovine 6S procarboxypeptidase A can be dissociated into its three subunits by acylation with dimethyl maleic anhydride. The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same residues in bovine chymotrypsinogen A and C (subunit II) and also in proelastase A of the African lungfish. Therefore, this subunit is likely to be a chymotrypsinogen or proelastase-A-like zymogen which has lost the ability to be activated on account of a deletion of the N-terminal residues from half-cystine 1 to valine 17. Like other pancreatic zymogens, subunit III appears to possess a weakly functional active site.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>237272</pmid><doi>10.1073/pnas.72.6.2442</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1975-06, Vol.72 (6), p.2442-2445 |
| issn | 0027-8424 1091-6490 |
| language | eng |
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| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Active sites Acylation Amino Acid Sequence Amino Acids - analysis Anhydrides Animals Biochemistry Carboxypeptidases - analysis Cattle Chemical Phenomena Chemistry Chromatography, DEAE-Cellulose Chromatography, Gel Condensation Endopeptidases Enzyme Precursors - analysis Hydrogen-Ion Concentration Macromolecular Substances Maleates Pancreas Pancreas - enzymology Peptides - analysis Peptides - isolation & purification Proteins Trimers Ungulates Zymogens |
| title | Dissociation of Bovine 6S Procarboxypeptidase A by Reversible Condensation with 2,3-dimethyl Maleic Anhydride: Application to the Partial Characterization of Subunit III |
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