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Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown
The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide, the activated residue was specifically labeled by the...
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| Published in: | The Journal of biological chemistry 1981-02, Vol.256 (4), p.1525-1528 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c430t-fc2b41864d7fdbd6e9181e488bddb2624c639c5ffb6b1b1b69f76389c73f5b313 |
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| cites | cdi_FETCH-LOGICAL-c430t-fc2b41864d7fdbd6e9181e488bddb2624c639c5ffb6b1b1b69f76389c73f5b313 |
| container_end_page | 1528 |
| container_issue | 4 |
| container_start_page | 1525 |
| container_title | The Journal of biological chemistry |
| container_volume | 256 |
| creator | Hershko, A Ciechanover, A Rose, I A |
| description | The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with
proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide,
the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following
acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde,
and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography.
These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine. |
| doi_str_mv | 10.1016/S0021-9258(19)69833-9 |
| format | article |
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proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide,
the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following
acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde,
and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography.
These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)69833-9</identifier><identifier>PMID: 6257674</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenosine Triphosphate ; Amino Acids - analysis ; Animals ; Borohydrides ; Chromosomal Proteins, Non-Histone - blood ; Erythrocytes - analysis ; Glycine - analysis ; Humans ; Rabbits ; Reticulocytes - enzymology ; Tritium ; Ubiquitins</subject><ispartof>The Journal of biological chemistry, 1981-02, Vol.256 (4), p.1525-1528</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c430t-fc2b41864d7fdbd6e9181e488bddb2624c639c5ffb6b1b1b69f76389c73f5b313</citedby><cites>FETCH-LOGICAL-c430t-fc2b41864d7fdbd6e9181e488bddb2624c639c5ffb6b1b1b69f76389c73f5b313</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/6257674$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hershko, A</creatorcontrib><creatorcontrib>Ciechanover, A</creatorcontrib><creatorcontrib>Rose, I A</creatorcontrib><title>Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with
proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide,
the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following
acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde,
and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography.
These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.</description><subject>Adenosine Triphosphate</subject><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Borohydrides</subject><subject>Chromosomal Proteins, Non-Histone - blood</subject><subject>Erythrocytes - analysis</subject><subject>Glycine - analysis</subject><subject>Humans</subject><subject>Rabbits</subject><subject>Reticulocytes - enzymology</subject><subject>Tritium</subject><subject>Ubiquitins</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><recordid>eNo9kEtLw0AQxxdRaq1-hELwIHqIZp_JHqX4KAgKVvC2ZHdn7WqTjdnU0m9v-tCZwzAz_3nwQ2iMs2ucYXHzmmUEp5Lw4hLLKyELSlN5gIY4K2hKOX4_RMN_yTE6ifEz641JPEADQXgucjZEMLVQd955U3Y-1ElwSTeHpDSd_-lD5evQJ94mLURvl_AnaMJi3UDTebst3c5eUgsN1JttSdOGDnyd6BbKLxtW9Sk6cuUiwtk-jtDb_d1s8pg-PT9MJ7dPqWE061JniGa4EMzmzmorQOICAysKba0mgjAjqDTcOS007l1IlwtaSJNTxzXFdIQudnv7D76XEDtV-WhgsShrCMuocs5JnjPeC_lOaNoQYwtONa2vynatcKY2eNUWr9qwU1iqLV4l-7nx_sBSV2D_p_Y8-_75rj_3H_OVb0FpH8wcKkW4UExhTjj9Bea4gpE</recordid><startdate>19810225</startdate><enddate>19810225</enddate><creator>Hershko, A</creator><creator>Ciechanover, A</creator><creator>Rose, I A</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>19810225</creationdate><title>Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown</title><author>Hershko, A ; Ciechanover, A ; Rose, I A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c430t-fc2b41864d7fdbd6e9181e488bddb2624c639c5ffb6b1b1b69f76389c73f5b313</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Adenosine Triphosphate</topic><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Borohydrides</topic><topic>Chromosomal Proteins, Non-Histone - blood</topic><topic>Erythrocytes - analysis</topic><topic>Glycine - analysis</topic><topic>Humans</topic><topic>Rabbits</topic><topic>Reticulocytes - enzymology</topic><topic>Tritium</topic><topic>Ubiquitins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hershko, A</creatorcontrib><creatorcontrib>Ciechanover, A</creatorcontrib><creatorcontrib>Rose, I 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>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hershko, A</au><au>Ciechanover, A</au><au>Rose, I A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1981-02-25</date><risdate>1981</risdate><volume>256</volume><issue>4</issue><spage>1525</spage><epage>1528</epage><pages>1525-1528</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The heat-stable polypeptide of the ATP-dependent proteolytic system was previously found to form covalent conjugates with
proteins and to be activated by ATP in an adenylylation mechanism. To identify the functional amino acid of the polypeptide,
the activated residue was specifically labeled by the reductive cleavage of the intermediate with [3H]borohydride. Following
acid hydrolysis, the reduced labeled derivative was found to be completely oxidizable by periodate with formation of [3H]formaldehyde,
and was identified as ethanolamine by thin layer chromatography, electrophoresis, and amino acid analyzer chromatography.
These results indicate that the activated amino acid residue of the polypeptide is COOH-terminal glycine.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6257674</pmid><doi>10.1016/S0021-9258(19)69833-9</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1981-02, Vol.256 (4), p.1525-1528 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75527745 |
| source | Elsevier ScienceDirect Journals |
| subjects | Adenosine Triphosphate Amino Acids - analysis Animals Borohydrides Chromosomal Proteins, Non-Histone - blood Erythrocytes - analysis Glycine - analysis Humans Rabbits Reticulocytes - enzymology Tritium Ubiquitins |
| title | Identification of the active amino acid residue of the polypeptide of ATP-dependent protein breakdown |
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