Characterization and amino acid sequence of a fatty acid-binding protein from human heart
The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation of CNBr, BNPS-skatole [3'-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides,...
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Veröffentlicht in: | Biochemical journal 1988-05, Vol.252 (1), p.191-198 |
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description | The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation of CNBr, BNPS-skatole [3'-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides, and by digestion of the protein with carboxypeptidase A. The sequence of the blocked N-terminal tryptic peptide from citraconylated protein was determined by collisionally induced decomposition mass spectrometry. The protein contains 132 amino acid residues, is enriched with respect to threonine and lysine, lacks cysteine, has an acetylated valine residue at the N-terminus, and has an Mr of 14768 and an isoelectric point of 5.25. This protein contains two short internal repeated sequences from residues 48-54 and from residues 114-119 located within regions of predicted beta-structure and decreasing hydrophobicity. These short repeats are contained within two longer repeated regions from residues 48-60 and residues 114-125, which display 62% sequence similarity. These regions could accommodate the charged and uncharged moieties of long-chain fatty acids and may represent fatty acid-binding domains consistent with the finding that human heart fatty acid-binding protein binds 2 mol of oleate or palmitate/mol of protein. Detailed evidence for the amino acid sequences of the peptides has been deposited as Supplementary Publication SUP 50143 (23 pages) at the British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5. |
doi_str_mv | 10.1042/bj2520191 |
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The sequence of the blocked N-terminal tryptic peptide from citraconylated protein was determined by collisionally induced decomposition mass spectrometry. The protein contains 132 amino acid residues, is enriched with respect to threonine and lysine, lacks cysteine, has an acetylated valine residue at the N-terminus, and has an Mr of 14768 and an isoelectric point of 5.25. This protein contains two short internal repeated sequences from residues 48-54 and from residues 114-119 located within regions of predicted beta-structure and decreasing hydrophobicity. These short repeats are contained within two longer repeated regions from residues 48-60 and residues 114-125, which display 62% sequence similarity. These regions could accommodate the charged and uncharged moieties of long-chain fatty acids and may represent fatty acid-binding domains consistent with the finding that human heart fatty acid-binding protein binds 2 mol of oleate or palmitate/mol of protein. Detailed evidence for the amino acid sequences of the peptides has been deposited as Supplementary Publication SUP 50143 (23 pages) at the British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj2520191</identifier><identifier>PMID: 3421901</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Carrier Proteins - isolation & purification ; Carrier Proteins - metabolism ; Chromatography, Gel ; Circular Dichroism ; fatty acid binding-protein ; Fatty Acid-Binding Protein 7 ; Fatty Acid-Binding Proteins ; Fatty Acids - metabolism ; heart ; Humans ; man ; Mass Spectrometry ; Molecular Sequence Data ; Myocardium - analysis ; Neoplasm Proteins ; Tumor Suppressor Proteins</subject><ispartof>Biochemical journal, 1988-05, Vol.252 (1), p.191-198</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c401t-e1cd5f0b30de7a9c6f29dd2efc4e59c6182239463942beb99ad266ff29b880083</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1149123/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1149123/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3421901$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Offner, G D</creatorcontrib><creatorcontrib>Brecher, P</creatorcontrib><creatorcontrib>Sawlivich, W B</creatorcontrib><creatorcontrib>Costello, C E</creatorcontrib><creatorcontrib>Troxler, R F</creatorcontrib><title>Characterization and amino acid sequence of a fatty acid-binding protein from human heart</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation of CNBr, BNPS-skatole [3'-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides, and by digestion of the protein with carboxypeptidase A. The sequence of the blocked N-terminal tryptic peptide from citraconylated protein was determined by collisionally induced decomposition mass spectrometry. The protein contains 132 amino acid residues, is enriched with respect to threonine and lysine, lacks cysteine, has an acetylated valine residue at the N-terminus, and has an Mr of 14768 and an isoelectric point of 5.25. This protein contains two short internal repeated sequences from residues 48-54 and from residues 114-119 located within regions of predicted beta-structure and decreasing hydrophobicity. These short repeats are contained within two longer repeated regions from residues 48-60 and residues 114-125, which display 62% sequence similarity. These regions could accommodate the charged and uncharged moieties of long-chain fatty acids and may represent fatty acid-binding domains consistent with the finding that human heart fatty acid-binding protein binds 2 mol of oleate or palmitate/mol of protein. Detailed evidence for the amino acid sequences of the peptides has been deposited as Supplementary Publication SUP 50143 (23 pages) at the British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5.</description><subject>Amino Acid Sequence</subject><subject>Carrier Proteins - isolation & purification</subject><subject>Carrier Proteins - metabolism</subject><subject>Chromatography, Gel</subject><subject>Circular Dichroism</subject><subject>fatty acid binding-protein</subject><subject>Fatty Acid-Binding Protein 7</subject><subject>Fatty Acid-Binding Proteins</subject><subject>Fatty Acids - metabolism</subject><subject>heart</subject><subject>Humans</subject><subject>man</subject><subject>Mass Spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Myocardium - analysis</subject><subject>Neoplasm Proteins</subject><subject>Tumor Suppressor Proteins</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtrHDEQhEVIsDd2DvkBAZ0CPkzSrdE8dDGExXmAIZfk4JPo0cMrsyOtJa3B-fWZxMvinHJomqY-imqKsbcIHxCk-DjdiU4AKnzBVigHaMZBjC_ZCkQvmx4EnrLXpdwBoAQJJ-yklQIV4IrdrDeUyVSXwy-qIUVO0XKaQ0ycTLC8uPu9i8bx5DlxT7U-_hWaKUQb4i3f5VRdiNznNPPNfqbIN45yPWevPG2Le3PYZ-zn56sf66_N9fcv39afrhsjAWvj0NjOw9SCdQMp03uhrBXOG-m65cRRiFbJfhkxuUkpsqLv_UJN4wgwtmfs8sl3t59mZ42LNdNW73KYKT_qREH_q8Sw0bfpQSNKhaJdDN4fDHJafi1Vz6EYt91SdGlf9DDKFjr5fxA7HAYFcgEvnkCTUynZ-WMaBP2nMH0sbGHfPY9_JA8Ntb8BV5qRxA</recordid><startdate>19880515</startdate><enddate>19880515</enddate><creator>Offner, G D</creator><creator>Brecher, P</creator><creator>Sawlivich, W B</creator><creator>Costello, C E</creator><creator>Troxler, R F</creator><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>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19880515</creationdate><title>Characterization and amino acid sequence of a fatty acid-binding protein from human heart</title><author>Offner, G D ; Brecher, P ; Sawlivich, W B ; Costello, C E ; Troxler, R F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-e1cd5f0b30de7a9c6f29dd2efc4e59c6182239463942beb99ad266ff29b880083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>Carrier Proteins - isolation & purification</topic><topic>Carrier Proteins - metabolism</topic><topic>Chromatography, Gel</topic><topic>Circular Dichroism</topic><topic>fatty acid binding-protein</topic><topic>Fatty Acid-Binding Protein 7</topic><topic>Fatty Acid-Binding Proteins</topic><topic>Fatty Acids - metabolism</topic><topic>heart</topic><topic>Humans</topic><topic>man</topic><topic>Mass Spectrometry</topic><topic>Molecular Sequence Data</topic><topic>Myocardium - analysis</topic><topic>Neoplasm Proteins</topic><topic>Tumor Suppressor Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Offner, G D</creatorcontrib><creatorcontrib>Brecher, P</creatorcontrib><creatorcontrib>Sawlivich, W B</creatorcontrib><creatorcontrib>Costello, C E</creatorcontrib><creatorcontrib>Troxler, R F</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Offner, G D</au><au>Brecher, P</au><au>Sawlivich, W B</au><au>Costello, C E</au><au>Troxler, R F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and amino acid sequence of a fatty acid-binding protein from human heart</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1988-05-15</date><risdate>1988</risdate><volume>252</volume><issue>1</issue><spage>191</spage><epage>198</epage><pages>191-198</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>The complete amino acid sequence of a fatty acid-binding protein from human heart was determined by automated Edman degradation of CNBr, BNPS-skatole [3'-bromo-3-methyl-2-(2-nitrobenzenesulphenyl)indolenine], hydroxylamine, Staphylococcus aureus V8 proteinase, tryptic and chymotryptic peptides, and by digestion of the protein with carboxypeptidase A. The sequence of the blocked N-terminal tryptic peptide from citraconylated protein was determined by collisionally induced decomposition mass spectrometry. The protein contains 132 amino acid residues, is enriched with respect to threonine and lysine, lacks cysteine, has an acetylated valine residue at the N-terminus, and has an Mr of 14768 and an isoelectric point of 5.25. This protein contains two short internal repeated sequences from residues 48-54 and from residues 114-119 located within regions of predicted beta-structure and decreasing hydrophobicity. These short repeats are contained within two longer repeated regions from residues 48-60 and residues 114-125, which display 62% sequence similarity. These regions could accommodate the charged and uncharged moieties of long-chain fatty acids and may represent fatty acid-binding domains consistent with the finding that human heart fatty acid-binding protein binds 2 mol of oleate or palmitate/mol of protein. Detailed evidence for the amino acid sequences of the peptides has been deposited as Supplementary Publication SUP 50143 (23 pages) at the British Library Lending Division, Boston Spa, Yorkshire LS23 7BQ, U.K., from whom copies may be obtained as indicated in Biochem. J. (1988) 249, 5.</abstract><cop>England</cop><pmid>3421901</pmid><doi>10.1042/bj2520191</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Carrier Proteins - isolation & purification Carrier Proteins - metabolism Chromatography, Gel Circular Dichroism fatty acid binding-protein Fatty Acid-Binding Protein 7 Fatty Acid-Binding Proteins Fatty Acids - metabolism heart Humans man Mass Spectrometry Molecular Sequence Data Myocardium - analysis Neoplasm Proteins Tumor Suppressor Proteins |
title | Characterization and amino acid sequence of a fatty acid-binding protein from human heart |
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