Covalent structural analysis of yeast inorganic pyrophosphatase

The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99). This information coupled with that derived from earlier structura...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1978-02, Vol.253 (3), p.889-897
Main Authors: Cohen, S A, Sterner, R, Keim, P S, Heinrikson, R L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Peptide Fragments
Pyrophosphatases
Saccharomyces cerevisiae - enzymology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c376t-6b8cdda0cddd50b5e59775d550cfc8f31e0f5dd1bb6265ed9334ca2e29a8f24f3
cites cdi_FETCH-LOGICAL-c376t-6b8cdda0cddd50b5e59775d550cfc8f31e0f5dd1bb6265ed9334ca2e29a8f24f3
container_end_page 897
container_issue 3
container_start_page 889
container_title The Journal of biological chemistry
container_volume 253
creator Cohen, S A
Sterner, R
Keim, P S
Heinrikson, R L
description The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99). This information coupled with that derived from earlier structural studies of the enzyme (Sterner, R., AND Heinrikson, R.L. (1975) Arch. Biochem. Biophys. 165, 693-703) provides the complete covalent structure of the pyrophosphatase subunit. The majority of the sequence data was derived from automated Edman degradation of the intact cyanogen bromide fragments and the large tryptic peptides obtained from citraconylated derivates in which cleavages were restricted to arginyl residues. The structural determination was completed by analysis of tryptic and chymotryptic peptides from the decitraconylated fragments. The monomer peptide chain contains 285 amino acid residues and the molecular weight calculated from the sequence analysis is 32,042.
doi_str_mv 10.1016/S0021-9258(17)38188-7
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_83721087</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>83721087</sourcerecordid><originalsourceid>FETCH-LOGICAL-c376t-6b8cdda0cddd50b5e59775d550cfc8f31e0f5dd1bb6265ed9334ca2e29a8f24f3</originalsourceid><addsrcrecordid>eNo9kElPwzAQhS3EVgr_AKRwQXAIeIlj54RQxSZV4gBI3CzHSxOUxMFOQPn3pE3VOcwc3nszmg-ACwRvEUTp3TuEGMUZpvwasRvCEecx2wMzBDmJCUVf-2C2sxyDkxC-4VhJho7AIUlgkqIZuF-4X1mZpotC53vV9V5WkWxkNYQyRM5Gg5Ghi8rG-ZVsShW1g3dt4UJbyE4GcwoOrKyCOdvOOfh8evxYvMTLt-fXxcMyVoSlXZzmXGkt4dg0hTk1NGOMakqhsopbggy0VGuU5ylOqdEZIYmS2OBMcosTS-bgatrbevfTm9CJugzKVJVsjOuD4ITh8XE2GulkVN6F4I0VrS9r6QeBoFhzExtuYg1FICY23MQ6d7490Oe10bvUBGqULye5KFfFX-mNyEunClMLTIkggvOM_APzq3Wh</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83721087</pqid></control><display><type>article</type><title>Covalent structural analysis of yeast inorganic pyrophosphatase</title><source>ScienceDirect Journals</source><creator>Cohen, S A ; Sterner, R ; Keim, P S ; Heinrikson, R L</creator><creatorcontrib>Cohen, S A ; Sterner, R ; Keim, P S ; Heinrikson, R L</creatorcontrib><description>The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99). This information coupled with that derived from earlier structural studies of the enzyme (Sterner, R., AND Heinrikson, R.L. (1975) Arch. Biochem. Biophys. 165, 693-703) provides the complete covalent structure of the pyrophosphatase subunit. The majority of the sequence data was derived from automated Edman degradation of the intact cyanogen bromide fragments and the large tryptic peptides obtained from citraconylated derivates in which cleavages were restricted to arginyl residues. The structural determination was completed by analysis of tryptic and chymotryptic peptides from the decitraconylated fragments. The monomer peptide chain contains 285 amino acid residues and the molecular weight calculated from the sequence analysis is 32,042.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(17)38188-7</identifier><identifier>PMID: 340461</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Peptide Fragments ; Pyrophosphatases ; Saccharomyces cerevisiae - enzymology</subject><ispartof>The Journal of biological chemistry, 1978-02, Vol.253 (3), p.889-897</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c376t-6b8cdda0cddd50b5e59775d550cfc8f31e0f5dd1bb6265ed9334ca2e29a8f24f3</citedby><cites>FETCH-LOGICAL-c376t-6b8cdda0cddd50b5e59775d550cfc8f31e0f5dd1bb6265ed9334ca2e29a8f24f3</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/340461$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cohen, S A</creatorcontrib><creatorcontrib>Sterner, R</creatorcontrib><creatorcontrib>Keim, P S</creatorcontrib><creatorcontrib>Heinrikson, R L</creatorcontrib><title>Covalent structural analysis of yeast inorganic pyrophosphatase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99). This information coupled with that derived from earlier structural studies of the enzyme (Sterner, R., AND Heinrikson, R.L. (1975) Arch. Biochem. Biophys. 165, 693-703) provides the complete covalent structure of the pyrophosphatase subunit. The majority of the sequence data was derived from automated Edman degradation of the intact cyanogen bromide fragments and the large tryptic peptides obtained from citraconylated derivates in which cleavages were restricted to arginyl residues. The structural determination was completed by analysis of tryptic and chymotryptic peptides from the decitraconylated fragments. The monomer peptide chain contains 285 amino acid residues and the molecular weight calculated from the sequence analysis is 32,042.</description><subject>Amino Acid Sequence</subject><subject>Peptide Fragments</subject><subject>Pyrophosphatases</subject><subject>Saccharomyces cerevisiae - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><recordid>eNo9kElPwzAQhS3EVgr_AKRwQXAIeIlj54RQxSZV4gBI3CzHSxOUxMFOQPn3pE3VOcwc3nszmg-ACwRvEUTp3TuEGMUZpvwasRvCEecx2wMzBDmJCUVf-2C2sxyDkxC-4VhJho7AIUlgkqIZuF-4X1mZpotC53vV9V5WkWxkNYQyRM5Gg5Ghi8rG-ZVsShW1g3dt4UJbyE4GcwoOrKyCOdvOOfh8evxYvMTLt-fXxcMyVoSlXZzmXGkt4dg0hTk1NGOMakqhsopbggy0VGuU5ylOqdEZIYmS2OBMcosTS-bgatrbevfTm9CJugzKVJVsjOuD4ITh8XE2GulkVN6F4I0VrS9r6QeBoFhzExtuYg1FICY23MQ6d7490Oe10bvUBGqULye5KFfFX-mNyEunClMLTIkggvOM_APzq3Wh</recordid><startdate>19780210</startdate><enddate>19780210</enddate><creator>Cohen, S A</creator><creator>Sterner, R</creator><creator>Keim, P S</creator><creator>Heinrikson, R L</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>19780210</creationdate><title>Covalent structural analysis of yeast inorganic pyrophosphatase</title><author>Cohen, S A ; Sterner, R ; Keim, P S ; Heinrikson, R L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c376t-6b8cdda0cddd50b5e59775d550cfc8f31e0f5dd1bb6265ed9334ca2e29a8f24f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Amino Acid Sequence</topic><topic>Peptide Fragments</topic><topic>Pyrophosphatases</topic><topic>Saccharomyces cerevisiae - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cohen, S A</creatorcontrib><creatorcontrib>Sterner, R</creatorcontrib><creatorcontrib>Keim, P S</creatorcontrib><creatorcontrib>Heinrikson, R L</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>Cohen, S A</au><au>Sterner, R</au><au>Keim, P S</au><au>Heinrikson, R L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Covalent structural analysis of yeast inorganic pyrophosphatase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1978-02-10</date><risdate>1978</risdate><volume>253</volume><issue>3</issue><spage>889</spage><epage>897</epage><pages>889-897</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The present paper describes the amino acid sequence analysis of the internal and COOH-terminal cyanogen bromide fragments of yeast inorganic pyrophosphatase (Sterner, R., Noyes, C., and Heinrikson, R.L. (1974) Biochemistry 13, 91-99). This information coupled with that derived from earlier structural studies of the enzyme (Sterner, R., AND Heinrikson, R.L. (1975) Arch. Biochem. Biophys. 165, 693-703) provides the complete covalent structure of the pyrophosphatase subunit. The majority of the sequence data was derived from automated Edman degradation of the intact cyanogen bromide fragments and the large tryptic peptides obtained from citraconylated derivates in which cleavages were restricted to arginyl residues. The structural determination was completed by analysis of tryptic and chymotryptic peptides from the decitraconylated fragments. The monomer peptide chain contains 285 amino acid residues and the molecular weight calculated from the sequence analysis is 32,042.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>340461</pmid><doi>10.1016/S0021-9258(17)38188-7</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9258
ispartof The Journal of biological chemistry, 1978-02, Vol.253 (3), p.889-897
issn 0021-9258
1083-351X
language eng
recordid cdi_proquest_miscellaneous_83721087
source ScienceDirect Journals
subjects Amino Acid Sequence
Peptide Fragments
Pyrophosphatases
Saccharomyces cerevisiae - enzymology
title Covalent structural analysis of yeast inorganic pyrophosphatase
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T19%3A28%3A47IST&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=Covalent%20structural%20analysis%20of%20yeast%20inorganic%20pyrophosphatase&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Cohen,%20S%20A&rft.date=1978-02-10&rft.volume=253&rft.issue=3&rft.spage=889&rft.epage=897&rft.pages=889-897&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1016/S0021-9258(17)38188-7&rft_dat=%3Cproquest_cross%3E83721087%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c376t-6b8cdda0cddd50b5e59775d550cfc8f31e0f5dd1bb6265ed9334ca2e29a8f24f3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=83721087&rft_id=info:pmid/340461&rfr_iscdi=true