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Disulfide Bridges in an α-Amylase Inhibitor from Wheat Kernel
An α-amylase inhibitor (0.53-inhibitor) was digested with pepsin and the cystine-containing peptides were isolated by SP-Sephadex C-25 column chromatography and high voltage paper electrophoresis. Amino acid compositions and partial sequences of these peptides and amino acid compositions of the pept...
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Published in: | Journal of biochemistry (Tokyo) 1983-01, Vol.94 (3), p.865-870 |
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container_title | Journal of biochemistry (Tokyo) |
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creator | MAEDA, Koji WAKABAYASHI, Sadao MATSUBARA, Hiroshi |
description | An α-amylase inhibitor (0.53-inhibitor) was digested with pepsin and the cystine-containing peptides were isolated by SP-Sephadex C-25 column chromatography and high voltage paper electrophoresis. Amino acid compositions and partial sequences of these peptides and amino acid compositions of the peptides separated after performic acid oxidation revealed the presence of 4 disulfide bonds in the inhibitor. They were formed between residues 6 and 115, 20 and either 41 or 42, 99 and either 41 or 42, and 28 and 83. The disulfide bond partners of residues 20 and 99 were not conclusively determined because of the difficulty of cleavage of the Cys-Cys bond at residues 41 and 42. Among 9 cysteines in this inhibitor Cys-54 must be in a free form, since no evidence was obtained for its contribution to disulfide bond formation. |
doi_str_mv | 10.1093/oxfordjournals.jbchem.a134429 |
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Amino acid compositions and partial sequences of these peptides and amino acid compositions of the peptides separated after performic acid oxidation revealed the presence of 4 disulfide bonds in the inhibitor. They were formed between residues 6 and 115, 20 and either 41 or 42, 99 and either 41 or 42, and 28 and 83. The disulfide bond partners of residues 20 and 99 were not conclusively determined because of the difficulty of cleavage of the Cys-Cys bond at residues 41 and 42. Among 9 cysteines in this inhibitor Cys-54 must be in a free form, since no evidence was obtained for its contribution to disulfide bond formation.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a134429</identifier><identifier>PMID: 6605967</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>alpha -amylase inhibitor ; alpha-Amylases - antagonists & inhibitors ; Amino Acid Sequence ; Cysteine ; disulfide bonds ; Disulfides - analysis ; Enzyme Inhibitors - isolation & purification ; Peptide Fragments - analysis ; Plant Proteins - isolation & purification ; Protein Conformation ; Seeds - analysis ; Triticum</subject><ispartof>Journal of biochemistry (Tokyo), 1983-01, Vol.94 (3), p.865-870</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c462t-f82cec13ff6fca3ea024b70b9d1407da69e2b88e393dbb5b954ec78084a3c4503</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27915,27916</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6605967$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MAEDA, Koji</creatorcontrib><creatorcontrib>WAKABAYASHI, Sadao</creatorcontrib><creatorcontrib>MATSUBARA, Hiroshi</creatorcontrib><title>Disulfide Bridges in an α-Amylase Inhibitor from Wheat Kernel</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>An α-amylase inhibitor (0.53-inhibitor) was digested with pepsin and the cystine-containing peptides were isolated by SP-Sephadex C-25 column chromatography and high voltage paper electrophoresis. Amino acid compositions and partial sequences of these peptides and amino acid compositions of the peptides separated after performic acid oxidation revealed the presence of 4 disulfide bonds in the inhibitor. They were formed between residues 6 and 115, 20 and either 41 or 42, 99 and either 41 or 42, and 28 and 83. The disulfide bond partners of residues 20 and 99 were not conclusively determined because of the difficulty of cleavage of the Cys-Cys bond at residues 41 and 42. Among 9 cysteines in this inhibitor Cys-54 must be in a free form, since no evidence was obtained for its contribution to disulfide bond formation.</description><subject>alpha -amylase inhibitor</subject><subject>alpha-Amylases - antagonists & inhibitors</subject><subject>Amino Acid Sequence</subject><subject>Cysteine</subject><subject>disulfide bonds</subject><subject>Disulfides - analysis</subject><subject>Enzyme Inhibitors - isolation & purification</subject><subject>Peptide Fragments - analysis</subject><subject>Plant Proteins - isolation & purification</subject><subject>Protein Conformation</subject><subject>Seeds - analysis</subject><subject>Triticum</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><recordid>eNqFkM1OGzEUha2qiAbaR6g0G7qb4L-xxwuQAi0EEamLUhV1Y9mea-IwP2DPSMlj9UX6TAxKFIkVq6urc869Rx9CJwRPCVbstFv7LlarboitqdN0Zd0SmqkhjHOqPqAJkYXIqSjIRzTBmJJcUX7_CR2ltHpdKWOH6FAIXCghJ-j8e0hD7UMF2UUM1QOkLLSZabP___JZs6lNguymXQYb-i5mPnZN9mcJps9uIbZQf0YHfmwBX3bzGP2--nF3Oc8XP69vLmeL3HFB-9yX1IEjzHvhnWFgMOVWYqsqwrGsjFBAbVkCU6yytrCq4OBkiUtumOMFZsfo2_buU-yeB0i9bkJyUNemhW5IusRSYlXSd42ESYGxKEfj2dboYpdSBK-fYmhM3GiC9Sto_Ra03oLWO9Bj_uvu0WAbqPbpHdlRz7d6SD2s97KJj3pUZaHn93-1XNwVc_WLjrVeAHYpkPk</recordid><startdate>19830101</startdate><enddate>19830101</enddate><creator>MAEDA, Koji</creator><creator>WAKABAYASHI, Sadao</creator><creator>MATSUBARA, Hiroshi</creator><general>Oxford University Press</general><scope>BSCLL</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19830101</creationdate><title>Disulfide Bridges in an α-Amylase Inhibitor from Wheat Kernel</title><author>MAEDA, Koji ; WAKABAYASHI, Sadao ; MATSUBARA, Hiroshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c462t-f82cec13ff6fca3ea024b70b9d1407da69e2b88e393dbb5b954ec78084a3c4503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>alpha -amylase inhibitor</topic><topic>alpha-Amylases - antagonists & inhibitors</topic><topic>Amino Acid Sequence</topic><topic>Cysteine</topic><topic>disulfide bonds</topic><topic>Disulfides - analysis</topic><topic>Enzyme Inhibitors - isolation & purification</topic><topic>Peptide Fragments - analysis</topic><topic>Plant Proteins - isolation & purification</topic><topic>Protein Conformation</topic><topic>Seeds - analysis</topic><topic>Triticum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MAEDA, Koji</creatorcontrib><creatorcontrib>WAKABAYASHI, Sadao</creatorcontrib><creatorcontrib>MATSUBARA, Hiroshi</creatorcontrib><collection>Istex</collection><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>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MAEDA, Koji</au><au>WAKABAYASHI, Sadao</au><au>MATSUBARA, Hiroshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Disulfide Bridges in an α-Amylase Inhibitor from Wheat Kernel</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1983-01-01</date><risdate>1983</risdate><volume>94</volume><issue>3</issue><spage>865</spage><epage>870</epage><pages>865-870</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>An α-amylase inhibitor (0.53-inhibitor) was digested with pepsin and the cystine-containing peptides were isolated by SP-Sephadex C-25 column chromatography and high voltage paper electrophoresis. Amino acid compositions and partial sequences of these peptides and amino acid compositions of the peptides separated after performic acid oxidation revealed the presence of 4 disulfide bonds in the inhibitor. They were formed between residues 6 and 115, 20 and either 41 or 42, 99 and either 41 or 42, and 28 and 83. The disulfide bond partners of residues 20 and 99 were not conclusively determined because of the difficulty of cleavage of the Cys-Cys bond at residues 41 and 42. Among 9 cysteines in this inhibitor Cys-54 must be in a free form, since no evidence was obtained for its contribution to disulfide bond formation.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>6605967</pmid><doi>10.1093/oxfordjournals.jbchem.a134429</doi><tpages>6</tpages></addata></record> |
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source | J-STAGE (Japan Science & Technology Information Aggregator, Electronic) - Open Access English articles; Oxford University Press Archive |
subjects | alpha -amylase inhibitor alpha-Amylases - antagonists & inhibitors Amino Acid Sequence Cysteine disulfide bonds Disulfides - analysis Enzyme Inhibitors - isolation & purification Peptide Fragments - analysis Plant Proteins - isolation & purification Protein Conformation Seeds - analysis Triticum |
title | Disulfide Bridges in an α-Amylase Inhibitor from Wheat Kernel |
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