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The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. I. Tryptic peptides
A total of 25 tryptic peptides was isolated from the S-beta-carboxymethyl derivative of Clostridium pasteurianum iron protein (N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column chromatographic methods, as well as various asc...
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| Published in: | The Journal of biological chemistry 1977-10, Vol.252 (20), p.7081-7088 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| container_end_page | 7088 |
| container_issue | 20 |
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| container_title | The Journal of biological chemistry |
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| creator | Tanaka, M Haniu, M Yasunobu, K T |
| description | A total of 25 tryptic peptides was isolated from the S-beta-carboxymethyl derivative of Clostridium pasteurianum iron protein
(N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column
chromatographic methods, as well as various ascending paper chromatographic methods were adopted. Sequence studies of the
tryptic peptides were carried out mainly by a modified manual Edman degradation procedure and also by automated analysis,
carboxypeptidase digestion, and by hydrazinolysis. Thus, 242 residues (88.6%) out of a total of 273 amino acid residues were
sequenced in the present study. The sum of the amino acid residues in the tryptic peptides isolated from iron protein (N2)
accounted for the 273 amino acid residues present in the iron protein. |
| doi_str_mv | 10.1016/S0021-9258(19)66937-1 |
| format | article |
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(N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column
chromatographic methods, as well as various ascending paper chromatographic methods were adopted. Sequence studies of the
tryptic peptides were carried out mainly by a modified manual Edman degradation procedure and also by automated analysis,
carboxypeptidase digestion, and by hydrazinolysis. Thus, 242 residues (88.6%) out of a total of 273 amino acid residues were
sequenced in the present study. The sum of the amino acid residues in the tryptic peptides isolated from iron protein (N2)
accounted for the 273 amino acid residues present in the iron protein.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)66937-1</identifier><identifier>PMID: 561781</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Clostridium - enzymology ; Ferredoxins ; Nitrogenase ; Peptide Fragments - analysis ; Trypsin</subject><ispartof>The Journal of biological chemistry, 1977-10, Vol.252 (20), p.7081-7088</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2931-c9408c150b48d08572a60510e41c07e60dcc051b93a2a38dfc61430159cbadbc3</citedby><cites>FETCH-LOGICAL-c2931-c9408c150b48d08572a60510e41c07e60dcc051b93a2a38dfc61430159cbadbc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/561781$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tanaka, M</creatorcontrib><creatorcontrib>Haniu, M</creatorcontrib><creatorcontrib>Yasunobu, K T</creatorcontrib><title>The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. I. Tryptic peptides</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A total of 25 tryptic peptides was isolated from the S-beta-carboxymethyl derivative of Clostridium pasteurianum iron protein
(N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column
chromatographic methods, as well as various ascending paper chromatographic methods were adopted. Sequence studies of the
tryptic peptides were carried out mainly by a modified manual Edman degradation procedure and also by automated analysis,
carboxypeptidase digestion, and by hydrazinolysis. Thus, 242 residues (88.6%) out of a total of 273 amino acid residues were
sequenced in the present study. The sum of the amino acid residues in the tryptic peptides isolated from iron protein (N2)
accounted for the 273 amino acid residues present in the iron protein.</description><subject>Amino Acid Sequence</subject><subject>Clostridium - enzymology</subject><subject>Ferredoxins</subject><subject>Nitrogenase</subject><subject>Peptide Fragments - analysis</subject><subject>Trypsin</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1977</creationdate><recordtype>article</recordtype><recordid>eNo9kG9rFDEQxoNY9ax-A4VAQRTcc2az2U1eyqFtoeALT_BdyGbnepHbZJvsUvrtzfVK580wzPPMnx9jHxHWCNh--w1QY6VrqT6j_tK2WnQVvmArBCUqIfHvS7Z6lrxhb3P-ByUaja_ZK9lip3DF7rZ74nb0IXLr_MAz3S0UHPG445tDzHPyg19GPtk805K8DaXwKQY-pTiTD1-55S6OUwwU5qMr-DnFWwo205pfr_k2PUyzd3yikgbK79jZzh4yvX_K5-zPzx_bzVV18-vyevP9pnK1Flg53YByKKFv1ABKdrVtQSJQgw46amFwrtS9Fra2Qg0712IjAKV2vR16J87Zp9Pccmj5Kc9m9NnR4WADxSUb1UAnQKoilCehSzHnRDszJT_a9GAQzJG0eSRtjhgNavNI2mDxfXhasPQjDc-uE9rSvji19_52f-8Tmd5Ht6fR1LI2NZgOiuo_x0iFow</recordid><startdate>19771025</startdate><enddate>19771025</enddate><creator>Tanaka, M</creator><creator>Haniu, M</creator><creator>Yasunobu, K T</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>19771025</creationdate><title>The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. I. Tryptic peptides</title><author>Tanaka, M ; Haniu, M ; Yasunobu, K T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2931-c9408c150b48d08572a60510e41c07e60dcc051b93a2a38dfc61430159cbadbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1977</creationdate><topic>Amino Acid Sequence</topic><topic>Clostridium - enzymology</topic><topic>Ferredoxins</topic><topic>Nitrogenase</topic><topic>Peptide Fragments - analysis</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tanaka, M</creatorcontrib><creatorcontrib>Haniu, M</creatorcontrib><creatorcontrib>Yasunobu, K T</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>Tanaka, M</au><au>Haniu, M</au><au>Yasunobu, K T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. I. Tryptic peptides</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1977-10-25</date><risdate>1977</risdate><volume>252</volume><issue>20</issue><spage>7081</spage><epage>7088</epage><pages>7081-7088</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A total of 25 tryptic peptides was isolated from the S-beta-carboxymethyl derivative of Clostridium pasteurianum iron protein
(N2). In order to obtain the various peptides in pure state, a combination of gel permeation, cation and anion exchange column
chromatographic methods, as well as various ascending paper chromatographic methods were adopted. Sequence studies of the
tryptic peptides were carried out mainly by a modified manual Edman degradation procedure and also by automated analysis,
carboxypeptidase digestion, and by hydrazinolysis. Thus, 242 residues (88.6%) out of a total of 273 amino acid residues were
sequenced in the present study. The sum of the amino acid residues in the tryptic peptides isolated from iron protein (N2)
accounted for the 273 amino acid residues present in the iron protein.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>561781</pmid><doi>10.1016/S0021-9258(19)66937-1</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1977-10, Vol.252 (20), p.7081-7088 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_84073058 |
| source | ScienceDirect® |
| subjects | Amino Acid Sequence Clostridium - enzymology Ferredoxins Nitrogenase Peptide Fragments - analysis Trypsin |
| title | The amino acid sequence of Clostridium pasteurianum iron protein, a component of nitrogenase. I. Tryptic peptides |
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