Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor poylypeptide

Bovine immunodeficiency virus Gag proteins were purified from virions, and their amino acid sequences and molecular masses were determined. The matrix, capsid, and nucleocapsid (MA, CA, and NC, respectively) and three smaller proteins (p21, p3, and p2) were found to have molecular masses of 14.6. 24...

Full description

Saved in:
Bibliographic Details
Published in:Journal of virology 1994-11, Vol.68 (11)
Main Authors: Tobin, G.J, Sowder, R.C. II, Fabris, D, Hu, M.Y, Battles, J.K, Fenselau, C, Henderson, L.E, Gonda, M.A
Format: Article
Language:English
Subjects:
LENTIVIRINAE
PEPTIDE
PEPTIDOS
PESO MOLECULAR
POIDS MOLECULAIRE
PROTEINAS
PROTEINE
VIRUS DE LOS ANIMALES
VIRUS DES ANIMAUX
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page
container_issue 11
container_start_page
container_title Journal of virology
container_volume 68
creator Tobin, G.J
Sowder, R.C. II
Fabris, D
Hu, M.Y
Battles, J.K
Fenselau, C
Henderson, L.E
Gonda, M.A
description Bovine immunodeficiency virus Gag proteins were purified from virions, and their amino acid sequences and molecular masses were determined. The matrix, capsid, and nucleocapsid (MA, CA, and NC, respectively) and three smaller proteins (p21, p3, and p2) were found to have molecular masses of 14.6. 24.6, and 7.3 and 2.5, 2.7, and 1.9 kDa, respectively. The order of these six proteins in the Gag precursor, Pr53gag, is NH2-MA-p2L-CA-p3-NC-p2-COOH. In contrast to other retroviral MA proteins, the bovine immunodeficiency virus MA retains its N-terminal methionine and is not modified by fatty acids. In addition, the bovine immunodeficiency virus NC migrates as a 13-kDa protein in denaturing gel electrophoresis; however, its molecular mass was determined to be 7.3 kDa
format article
fullrecord <record><control><sourceid>fao</sourceid><recordid>TN_cdi_fao_agris_US9517161</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>US9517161</sourcerecordid><originalsourceid>FETCH-fao_agris_US95171613</originalsourceid><addsrcrecordid>eNp9jM1Kw0AUhYeiYNS-gKv7AoGZNqntsog_exXclevkJt4ymRvnJzBL39wi4tLVgfOd7yxUZfRuW7etac5UpfVqVbfr7duFuozxqLVpmk1Tqa_9yF4ALXcQ6TOTtwTo0ZXIEaSH9EEwBUkkriS2YB3hjMNP2WWb_kbvMrMn4HHMXjrq2fLprMDMIUd4xOFkkM0hSoBJiisTTYk7ulbnPbpIy9-8UjcP9y93T3WPcsAhcDy8Pu9ac2s2Zv0v_AatBkzO</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor poylypeptide</title><source>PubMed Central Free</source><source>American Society for Microbiology Journals</source><creator>Tobin, G.J ; Sowder, R.C. II ; Fabris, D ; Hu, M.Y ; Battles, J.K ; Fenselau, C ; Henderson, L.E ; Gonda, M.A</creator><creatorcontrib>Tobin, G.J ; Sowder, R.C. II ; Fabris, D ; Hu, M.Y ; Battles, J.K ; Fenselau, C ; Henderson, L.E ; Gonda, M.A</creatorcontrib><description>Bovine immunodeficiency virus Gag proteins were purified from virions, and their amino acid sequences and molecular masses were determined. The matrix, capsid, and nucleocapsid (MA, CA, and NC, respectively) and three smaller proteins (p21, p3, and p2) were found to have molecular masses of 14.6. 24.6, and 7.3 and 2.5, 2.7, and 1.9 kDa, respectively. The order of these six proteins in the Gag precursor, Pr53gag, is NH2-MA-p2L-CA-p3-NC-p2-COOH. In contrast to other retroviral MA proteins, the bovine immunodeficiency virus MA retains its N-terminal methionine and is not modified by fatty acids. In addition, the bovine immunodeficiency virus NC migrates as a 13-kDa protein in denaturing gel electrophoresis; however, its molecular mass was determined to be 7.3 kDa</description><identifier>ISSN: 0022-538X</identifier><identifier>EISSN: 1098-5514</identifier><language>eng</language><subject>LENTIVIRINAE ; PEPTIDE ; PEPTIDOS ; PESO MOLECULAR ; POIDS MOLECULAIRE ; PROTEINAS ; PROTEINE ; VIRUS DE LOS ANIMALES ; VIRUS DES ANIMAUX</subject><ispartof>Journal of virology, 1994-11, Vol.68 (11)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids></links><search><creatorcontrib>Tobin, G.J</creatorcontrib><creatorcontrib>Sowder, R.C. II</creatorcontrib><creatorcontrib>Fabris, D</creatorcontrib><creatorcontrib>Hu, M.Y</creatorcontrib><creatorcontrib>Battles, J.K</creatorcontrib><creatorcontrib>Fenselau, C</creatorcontrib><creatorcontrib>Henderson, L.E</creatorcontrib><creatorcontrib>Gonda, M.A</creatorcontrib><title>Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor poylypeptide</title><title>Journal of virology</title><description>Bovine immunodeficiency virus Gag proteins were purified from virions, and their amino acid sequences and molecular masses were determined. The matrix, capsid, and nucleocapsid (MA, CA, and NC, respectively) and three smaller proteins (p21, p3, and p2) were found to have molecular masses of 14.6. 24.6, and 7.3 and 2.5, 2.7, and 1.9 kDa, respectively. The order of these six proteins in the Gag precursor, Pr53gag, is NH2-MA-p2L-CA-p3-NC-p2-COOH. In contrast to other retroviral MA proteins, the bovine immunodeficiency virus MA retains its N-terminal methionine and is not modified by fatty acids. In addition, the bovine immunodeficiency virus NC migrates as a 13-kDa protein in denaturing gel electrophoresis; however, its molecular mass was determined to be 7.3 kDa</description><subject>LENTIVIRINAE</subject><subject>PEPTIDE</subject><subject>PEPTIDOS</subject><subject>PESO MOLECULAR</subject><subject>POIDS MOLECULAIRE</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>VIRUS DE LOS ANIMALES</subject><subject>VIRUS DES ANIMAUX</subject><issn>0022-538X</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><recordid>eNp9jM1Kw0AUhYeiYNS-gKv7AoGZNqntsog_exXclevkJt4ymRvnJzBL39wi4tLVgfOd7yxUZfRuW7etac5UpfVqVbfr7duFuozxqLVpmk1Tqa_9yF4ALXcQ6TOTtwTo0ZXIEaSH9EEwBUkkriS2YB3hjMNP2WWb_kbvMrMn4HHMXjrq2fLprMDMIUd4xOFkkM0hSoBJiisTTYk7ulbnPbpIy9-8UjcP9y93T3WPcsAhcDy8Pu9ac2s2Zv0v_AatBkzO</recordid><startdate>199411</startdate><enddate>199411</enddate><creator>Tobin, G.J</creator><creator>Sowder, R.C. II</creator><creator>Fabris, D</creator><creator>Hu, M.Y</creator><creator>Battles, J.K</creator><creator>Fenselau, C</creator><creator>Henderson, L.E</creator><creator>Gonda, M.A</creator><scope>FBQ</scope></search><sort><creationdate>199411</creationdate><title>Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor poylypeptide</title><author>Tobin, G.J ; Sowder, R.C. II ; Fabris, D ; Hu, M.Y ; Battles, J.K ; Fenselau, C ; Henderson, L.E ; Gonda, M.A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-fao_agris_US95171613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>LENTIVIRINAE</topic><topic>PEPTIDE</topic><topic>PEPTIDOS</topic><topic>PESO MOLECULAR</topic><topic>POIDS MOLECULAIRE</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>VIRUS DE LOS ANIMALES</topic><topic>VIRUS DES ANIMAUX</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tobin, G.J</creatorcontrib><creatorcontrib>Sowder, R.C. II</creatorcontrib><creatorcontrib>Fabris, D</creatorcontrib><creatorcontrib>Hu, M.Y</creatorcontrib><creatorcontrib>Battles, J.K</creatorcontrib><creatorcontrib>Fenselau, C</creatorcontrib><creatorcontrib>Henderson, L.E</creatorcontrib><creatorcontrib>Gonda, M.A</creatorcontrib><collection>AGRIS</collection><jtitle>Journal of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tobin, G.J</au><au>Sowder, R.C. II</au><au>Fabris, D</au><au>Hu, M.Y</au><au>Battles, J.K</au><au>Fenselau, C</au><au>Henderson, L.E</au><au>Gonda, M.A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor poylypeptide</atitle><jtitle>Journal of virology</jtitle><date>1994-11</date><risdate>1994</risdate><volume>68</volume><issue>11</issue><issn>0022-538X</issn><eissn>1098-5514</eissn><abstract>Bovine immunodeficiency virus Gag proteins were purified from virions, and their amino acid sequences and molecular masses were determined. The matrix, capsid, and nucleocapsid (MA, CA, and NC, respectively) and three smaller proteins (p21, p3, and p2) were found to have molecular masses of 14.6. 24.6, and 7.3 and 2.5, 2.7, and 1.9 kDa, respectively. The order of these six proteins in the Gag precursor, Pr53gag, is NH2-MA-p2L-CA-p3-NC-p2-COOH. In contrast to other retroviral MA proteins, the bovine immunodeficiency virus MA retains its N-terminal methionine and is not modified by fatty acids. In addition, the bovine immunodeficiency virus NC migrates as a 13-kDa protein in denaturing gel electrophoresis; however, its molecular mass was determined to be 7.3 kDa</abstract></addata></record>
fulltext fulltext
identifier ISSN: 0022-538X
ispartof Journal of virology, 1994-11, Vol.68 (11)
issn 0022-538X
1098-5514
language eng
recordid cdi_fao_agris_US9517161
source PubMed Central Free; American Society for Microbiology Journals
subjects LENTIVIRINAE
PEPTIDE
PEPTIDOS
PESO MOLECULAR
POIDS MOLECULAIRE
PROTEINAS
PROTEINE
VIRUS DE LOS ANIMALES
VIRUS DES ANIMAUX
title Amino acid sequence analysis of the proteolytic cleavage products of the bovine immunodeficiency virus Gag precursor poylypeptide
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T05%3A27%3A23IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-fao&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Amino%20acid%20sequence%20analysis%20of%20the%20proteolytic%20cleavage%20products%20of%20the%20bovine%20immunodeficiency%20virus%20Gag%20precursor%20poylypeptide&rft.jtitle=Journal%20of%20virology&rft.au=Tobin,%20G.J&rft.date=1994-11&rft.volume=68&rft.issue=11&rft.issn=0022-538X&rft.eissn=1098-5514&rft_id=info:doi/&rft_dat=%3Cfao%3EUS9517161%3C/fao%3E%3Cgrp_id%3Ecdi_FETCH-fao_agris_US95171613%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true