Isolation and amino acid sequence of two trypsin isoinhibitors from duck pancreas
DPTI II and DPTI IV, two trypsin inhibitors from duck pancreas, have been isolated by affinity chromatography on immobilized anhydrotrypsin, anion exchange and RP-HPLC. The complete amino acid sequence of both inhibitors was determined after reductive carboxymethylation and digestion with Staphyloco...
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| Veröffentlicht in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 1999-11, Vol.124 (3), p.281-288 |
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| container_title | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
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| creator | Wilimowska-Pelc, Anna Olczak, Mariusz Olichwier, Zofia Gładysz, Marta Wilusz, Tadeusz |
| description | DPTI II and DPTI IV, two trypsin inhibitors from duck pancreas, have been isolated by affinity chromatography on immobilized anhydrotrypsin, anion exchange and RP-HPLC. The complete amino acid sequence of both inhibitors was determined after reductive carboxymethylation and digestion with
Staphylococcus aureus V8 protease or trypsin. The inhibitors were each found to be a single polypeptide chain comprised of 69 amino acid residues and their molecular masses were estimated at 7687 Da for DPTI II and 7668 Da for DPTI IV. The only difference in amino acid sequence between the two inhibitors is the replacement of Arg for His residue in the C-terminal position of DPTI IV. |
| doi_str_mv | 10.1016/S0305-0491(99)00118-2 |
| format | Article |
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Staphylococcus aureus V8 protease or trypsin. The inhibitors were each found to be a single polypeptide chain comprised of 69 amino acid residues and their molecular masses were estimated at 7687 Da for DPTI II and 7668 Da for DPTI IV. The only difference in amino acid sequence between the two inhibitors is the replacement of Arg for His residue in the C-terminal position of DPTI IV.</description><identifier>ISSN: 1096-4959</identifier><identifier>ISSN: 0305-0491</identifier><identifier>EISSN: 1879-1107</identifier><identifier>DOI: 10.1016/S0305-0491(99)00118-2</identifier><identifier>PMID: 10631805</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Amino Acids - analysis ; Anatidae ; Animals ; Chromatography, Affinity ; Chromatography, High Pressure Liquid ; Duck pancreas ; Ducks ; Electrophoresis, Polyacrylamide Gel ; Freshwater ; Kazal-type trypsin inhibitor ; Molecular Sequence Data ; Molecular Weight ; Pancreas - chemistry ; Peptides - chemistry ; Peptides - isolation & purification ; Peptides - metabolism ; Protein Isoforms ; Sequence Analysis, Protein ; Serine Endopeptidases - metabolism ; Species Specificity ; trypsin inhibitors ; Trypsin Inhibitors - chemistry ; Trypsin Inhibitors - isolation & purification ; Trypsin Inhibitors - metabolism ; Trypsin Inhibitors - pharmacology</subject><ispartof>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1999-11, Vol.124 (3), p.281-288</ispartof><rights>1999 Elsevier Science Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c482t-335acb47a263d9d61f34fbd13e8910d62adf2e0e83d451d79899d0bc3484eb593</citedby><cites>FETCH-LOGICAL-c482t-335acb47a263d9d61f34fbd13e8910d62adf2e0e83d451d79899d0bc3484eb593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0305049199001182$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10631805$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wilimowska-Pelc, Anna</creatorcontrib><creatorcontrib>Olczak, Mariusz</creatorcontrib><creatorcontrib>Olichwier, Zofia</creatorcontrib><creatorcontrib>Gładysz, Marta</creatorcontrib><creatorcontrib>Wilusz, Tadeusz</creatorcontrib><title>Isolation and amino acid sequence of two trypsin isoinhibitors from duck pancreas</title><title>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</title><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><description>DPTI II and DPTI IV, two trypsin inhibitors from duck pancreas, have been isolated by affinity chromatography on immobilized anhydrotrypsin, anion exchange and RP-HPLC. The complete amino acid sequence of both inhibitors was determined after reductive carboxymethylation and digestion with
Staphylococcus aureus V8 protease or trypsin. The inhibitors were each found to be a single polypeptide chain comprised of 69 amino acid residues and their molecular masses were estimated at 7687 Da for DPTI II and 7668 Da for DPTI IV. The only difference in amino acid sequence between the two inhibitors is the replacement of Arg for His residue in the C-terminal position of DPTI IV.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Amino Acids - analysis</subject><subject>Anatidae</subject><subject>Animals</subject><subject>Chromatography, Affinity</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Duck pancreas</subject><subject>Ducks</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Freshwater</subject><subject>Kazal-type trypsin inhibitor</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Pancreas - chemistry</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - metabolism</subject><subject>Protein Isoforms</subject><subject>Sequence Analysis, Protein</subject><subject>Serine Endopeptidases - metabolism</subject><subject>Species Specificity</subject><subject>trypsin inhibitors</subject><subject>Trypsin Inhibitors - chemistry</subject><subject>Trypsin Inhibitors - isolation & purification</subject><subject>Trypsin Inhibitors - metabolism</subject><subject>Trypsin Inhibitors - pharmacology</subject><issn>1096-4959</issn><issn>0305-0491</issn><issn>1879-1107</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtv1TAQRiMEog_4CYBXqCxSZvyKZ1WhCmilSqgqXVuO7YDhJr7YuUX99-Q2XbDramZxvnmcpnmDcIqA-uMNCFAtSMITog8AiKblz5pDNB21iNA9X3og3UpSdNAc1foLQBgU-LI5QNACDajD5vqy5o2bU56YmwJzY5oycz4FVuOfXZx8ZHlg89_M5nK_rWliqeY0_Ux9mnOpbCh5ZGHnf7Otm3yJrr5qXgxuU-Prx3rc3H75_P38or369vXy_NNV66XhcyuEcr6XneNaBAoaByGHPqCIhhCC5i4MPEI0IkiFoSNDFKD3QhoZe0XiuHm_zt2WvFxaZzum6uNm46aYd9VqkoBGd0-C2OmO0KgFVCvoS661xMFuSxpdubcIdi_dPki3e-mWyD5It3zJvX1csOvHGP5LrZYX4N0KDC5b96Okam9vOKAATqrjcv_M2UrExdhdisVWn_b2QyrRzzbk9MQR_wBE2JqG</recordid><startdate>19991101</startdate><enddate>19991101</enddate><creator>Wilimowska-Pelc, Anna</creator><creator>Olczak, Mariusz</creator><creator>Olichwier, Zofia</creator><creator>Gładysz, Marta</creator><creator>Wilusz, Tadeusz</creator><general>Elsevier Inc</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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19991101</creationdate><title>Isolation and amino acid sequence of two trypsin isoinhibitors from duck pancreas</title><author>Wilimowska-Pelc, Anna ; Olczak, Mariusz ; Olichwier, Zofia ; Gładysz, Marta ; Wilusz, Tadeusz</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-335acb47a263d9d61f34fbd13e8910d62adf2e0e83d451d79899d0bc3484eb593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Amino Acids - analysis</topic><topic>Anatidae</topic><topic>Animals</topic><topic>Chromatography, Affinity</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Duck pancreas</topic><topic>Ducks</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Freshwater</topic><topic>Kazal-type trypsin inhibitor</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Pancreas - chemistry</topic><topic>Peptides - chemistry</topic><topic>Peptides - isolation & purification</topic><topic>Peptides - metabolism</topic><topic>Protein Isoforms</topic><topic>Sequence Analysis, Protein</topic><topic>Serine Endopeptidases - metabolism</topic><topic>Species Specificity</topic><topic>trypsin inhibitors</topic><topic>Trypsin Inhibitors - chemistry</topic><topic>Trypsin Inhibitors - isolation & purification</topic><topic>Trypsin Inhibitors - metabolism</topic><topic>Trypsin Inhibitors - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilimowska-Pelc, Anna</creatorcontrib><creatorcontrib>Olczak, Mariusz</creatorcontrib><creatorcontrib>Olichwier, Zofia</creatorcontrib><creatorcontrib>Gładysz, Marta</creatorcontrib><creatorcontrib>Wilusz, Tadeusz</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>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilimowska-Pelc, Anna</au><au>Olczak, Mariusz</au><au>Olichwier, Zofia</au><au>Gładysz, Marta</au><au>Wilusz, Tadeusz</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and amino acid sequence of two trypsin isoinhibitors from duck pancreas</atitle><jtitle>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</jtitle><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><date>1999-11-01</date><risdate>1999</risdate><volume>124</volume><issue>3</issue><spage>281</spage><epage>288</epage><pages>281-288</pages><issn>1096-4959</issn><issn>0305-0491</issn><eissn>1879-1107</eissn><abstract>DPTI II and DPTI IV, two trypsin inhibitors from duck pancreas, have been isolated by affinity chromatography on immobilized anhydrotrypsin, anion exchange and RP-HPLC. The complete amino acid sequence of both inhibitors was determined after reductive carboxymethylation and digestion with
Staphylococcus aureus V8 protease or trypsin. The inhibitors were each found to be a single polypeptide chain comprised of 69 amino acid residues and their molecular masses were estimated at 7687 Da for DPTI II and 7668 Da for DPTI IV. The only difference in amino acid sequence between the two inhibitors is the replacement of Arg for His residue in the C-terminal position of DPTI IV.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>10631805</pmid><doi>10.1016/S0305-0491(99)00118-2</doi><tpages>8</tpages></addata></record> |
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| ispartof | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1999-11, Vol.124 (3), p.281-288 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence amino acid sequences Amino Acids - analysis Anatidae Animals Chromatography, Affinity Chromatography, High Pressure Liquid Duck pancreas Ducks Electrophoresis, Polyacrylamide Gel Freshwater Kazal-type trypsin inhibitor Molecular Sequence Data Molecular Weight Pancreas - chemistry Peptides - chemistry Peptides - isolation & purification Peptides - metabolism Protein Isoforms Sequence Analysis, Protein Serine Endopeptidases - metabolism Species Specificity trypsin inhibitors Trypsin Inhibitors - chemistry Trypsin Inhibitors - isolation & purification Trypsin Inhibitors - metabolism Trypsin Inhibitors - pharmacology |
| title | Isolation and amino acid sequence of two trypsin isoinhibitors from duck pancreas |
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