Loading…

Amino acid sequence of honeybee prepromelittin synthesized in vitro

Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic f...

Full description

Saved in:
Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1978-02, Vol.75 (2), p.701-704
Main Authors: Suchanek, G, Kreil, G, Hermodson, M.A
Format: Article
Language:English
Subjects:
Citations: 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-c3891-e199cb46fc560a468342eb36ac3885bd9544ee3f29e9b19f96a2a4386b497bbc3
cites
container_end_page 704
container_issue 2
container_start_page 701
container_title Proceedings of the National Academy of Sciences - PNAS
container_volume 75
creator Suchanek, G
Kreil, G
Hermodson, M.A
description Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to melittin.
doi_str_mv 10.1073/pnas.75.2.701
format article
fullrecord <record><control><sourceid>jstor_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1073_pnas_75_2_701</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>67854</jstor_id><sourcerecordid>67854</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3891-e199cb46fc560a468342eb36ac3885bd9544ee3f29e9b19f96a2a4386b497bbc3</originalsourceid><addsrcrecordid>eNptkEtv1DAUhS3Eaygs2SAksoFdpn7FiRddVKMWKlViQbu2bM9Nx1ViB9tTMfx6PMp0VKSurKvvnOtzD0IfCV4S3LLTyeu0bJslXbaYvEALgiWpBZf4JVpgTNu645S_Re9SuscYy6bDb9Br2jLK6AKtzkfnQ6WtW1cJfm_BW6hCX22Ch50BqKYIUwwjDC5n56u083kDyf2FdVXGB5djeI9e9XpI8OHwnqDby4ub1Y_6-uf3q9X5dW1ZVyIBkdIaLnrbCKy56BinYJjQBXeNWcuGcwDWUwnSENlLoanmrBOGy9YYy07Q2bx32poR1hZ8jnpQU3SjjjsVtFP_E-826i48KE4Io7z4vx38MZRLU1ajSxaGQXsI26S6ElM0WBRhPQttDClF6I9_EKz2nat956ptFFWl86L__DTYUT2XXPDXA967HuGjW_XbYcjwJz9Z85yu4E8zvk85xCMXbdfsb_syw14Hpe-iS-r2Fy0uTGhHymHsHy8pp98</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>83896506</pqid></control><display><type>article</type><title>Amino acid sequence of honeybee prepromelittin synthesized in vitro</title><source>JSTOR Archival Journals and Primary Sources Collection</source><source>PubMed Central</source><creator>Suchanek, G ; Kreil, G ; Hermodson, M.A</creator><creatorcontrib>Suchanek, G ; Kreil, G ; Hermodson, M.A</creatorcontrib><description>Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to melittin.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.75.2.701</identifier><identifier>PMID: 273232</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Amino Acid Sequence ; Amino acids ; Animal glands ; Apis mellifera ; Bee Venoms - metabolism ; Bees ; Biochemistry ; Cell free system ; Electrophoresis ; In Vitro Techniques ; Material degradation ; Melitten - metabolism ; Messenger RNA ; Neutral amino acids ; Protein Biosynthesis ; Protein Precursors - biosynthesis ; RNA ; Venoms</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1978-02, Vol.75 (2), p.701-704</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3891-e199cb46fc560a468342eb36ac3885bd9544ee3f29e9b19f96a2a4386b497bbc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/75/2.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/67854$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/67854$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793,58238,58471</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/273232$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Suchanek, G</creatorcontrib><creatorcontrib>Kreil, G</creatorcontrib><creatorcontrib>Hermodson, M.A</creatorcontrib><title>Amino acid sequence of honeybee prepromelittin synthesized in vitro</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to melittin.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animal glands</subject><subject>Apis mellifera</subject><subject>Bee Venoms - metabolism</subject><subject>Bees</subject><subject>Biochemistry</subject><subject>Cell free system</subject><subject>Electrophoresis</subject><subject>In Vitro Techniques</subject><subject>Material degradation</subject><subject>Melitten - metabolism</subject><subject>Messenger RNA</subject><subject>Neutral amino acids</subject><subject>Protein Biosynthesis</subject><subject>Protein Precursors - biosynthesis</subject><subject>RNA</subject><subject>Venoms</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><recordid>eNptkEtv1DAUhS3Eaygs2SAksoFdpn7FiRddVKMWKlViQbu2bM9Nx1ViB9tTMfx6PMp0VKSurKvvnOtzD0IfCV4S3LLTyeu0bJslXbaYvEALgiWpBZf4JVpgTNu645S_Re9SuscYy6bDb9Br2jLK6AKtzkfnQ6WtW1cJfm_BW6hCX22Ch50BqKYIUwwjDC5n56u083kDyf2FdVXGB5djeI9e9XpI8OHwnqDby4ub1Y_6-uf3q9X5dW1ZVyIBkdIaLnrbCKy56BinYJjQBXeNWcuGcwDWUwnSENlLoanmrBOGy9YYy07Q2bx32poR1hZ8jnpQU3SjjjsVtFP_E-826i48KE4Io7z4vx38MZRLU1ajSxaGQXsI26S6ElM0WBRhPQttDClF6I9_EKz2nat956ptFFWl86L__DTYUT2XXPDXA967HuGjW_XbYcjwJz9Z85yu4E8zvk85xCMXbdfsb_syw14Hpe-iS-r2Fy0uTGhHymHsHy8pp98</recordid><startdate>19780201</startdate><enddate>19780201</enddate><creator>Suchanek, G</creator><creator>Kreil, G</creator><creator>Hermodson, M.A</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</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><scope>5PM</scope></search><sort><creationdate>19780201</creationdate><title>Amino acid sequence of honeybee prepromelittin synthesized in vitro</title><author>Suchanek, G ; Kreil, G ; Hermodson, M.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3891-e199cb46fc560a468342eb36ac3885bd9544ee3f29e9b19f96a2a4386b497bbc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animal glands</topic><topic>Apis mellifera</topic><topic>Bee Venoms - metabolism</topic><topic>Bees</topic><topic>Biochemistry</topic><topic>Cell free system</topic><topic>Electrophoresis</topic><topic>In Vitro Techniques</topic><topic>Material degradation</topic><topic>Melitten - metabolism</topic><topic>Messenger RNA</topic><topic>Neutral amino acids</topic><topic>Protein Biosynthesis</topic><topic>Protein Precursors - biosynthesis</topic><topic>RNA</topic><topic>Venoms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Suchanek, G</creatorcontrib><creatorcontrib>Kreil, G</creatorcontrib><creatorcontrib>Hermodson, M.A</creatorcontrib><collection>AGRIS</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><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>Suchanek, G</au><au>Kreil, G</au><au>Hermodson, M.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid sequence of honeybee prepromelittin synthesized in vitro</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1978-02-01</date><risdate>1978</risdate><volume>75</volume><issue>2</issue><spage>701</spage><epage>704</epage><pages>701-704</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Translation of melittin messenger RNA from queen bee venom glands in a cell-free system from wheat germ yielded prepromelittin. Sequence analysis of the labeled in vitro product was performed by automatic Edman degradation of the intact polypeptide as well as by analysis of some of its proteolytic fragments. Prepromelittin was shown to be composed of 70 amino acids, two of which have not been identified. The sequence of melittin is located in the COOH-terminal third of the polypeptide chain (residues 44-69). Prepromelittin starts with a very hydrophobic pre-region, probably 21 residues long, followed by a pro-part of unusual sequence, containing only alanine, proline, and acidic residues. At least three post-translational reactions are required to convert prepromelittin to melittin.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>273232</pmid><doi>10.1073/pnas.75.2.701</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0027-8424
ispartof Proceedings of the National Academy of Sciences - PNAS, 1978-02, Vol.75 (2), p.701-704
issn 0027-8424
1091-6490
language eng
recordid cdi_crossref_primary_10_1073_pnas_75_2_701
source JSTOR Archival Journals and Primary Sources Collection; PubMed Central
subjects Amino Acid Sequence
Amino acids
Animal glands
Apis mellifera
Bee Venoms - metabolism
Bees
Biochemistry
Cell free system
Electrophoresis
In Vitro Techniques
Material degradation
Melitten - metabolism
Messenger RNA
Neutral amino acids
Protein Biosynthesis
Protein Precursors - biosynthesis
RNA
Venoms
title Amino acid sequence of honeybee prepromelittin synthesized in vitro
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T02%3A06%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amino%20acid%20sequence%20of%20honeybee%20prepromelittin%20synthesized%20in%20vitro&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Suchanek,%20G&rft.date=1978-02-01&rft.volume=75&rft.issue=2&rft.spage=701&rft.epage=704&rft.pages=701-704&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.75.2.701&rft_dat=%3Cjstor_cross%3E67854%3C/jstor_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c3891-e199cb46fc560a468342eb36ac3885bd9544ee3f29e9b19f96a2a4386b497bbc3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=83896506&rft_id=info:pmid/273232&rft_jstor_id=67854&rfr_iscdi=true