Assignments of the disulphide bonds in the sweet-tasting protein thaumatin I
The disulphide linkages of the 16 half-cyteine residues in the sweet-tasting protein thaumatin have been investigated by enzymatic hydrolysis of the intact molecule. The peptides obtained after proteolytic cleavage with trypsin and pepsin, and in one case with chymotrypsin have been purified by gel...
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| Veröffentlicht in: | European journal of biochemistry 1984-01, Vol.144 (1), p.41-45 |
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| container_title | European journal of biochemistry |
| container_volume | 144 |
| creator | Van Der Wel, H Iyengar, R B Van Brouwershaven, J Van Wassenaar, PD Bel, W J Van Der Ouderaa, FJG |
| description | The disulphide linkages of the 16 half-cyteine residues in the sweet-tasting protein thaumatin have been investigated by enzymatic hydrolysis of the intact molecule. The peptides obtained after proteolytic cleavage with trypsin and pepsin, and in one case with chymotrypsin have been purified by gel filtration, high-performance liquid chromatography and peptide mapping by paper high-voltage electrophoresis in one direction and paper chromatography in the second dimension. Disulphide bonds appeared to be formed by cysteine residues in positions 9-204, 56-66, 71-77, 121-193, 126-177, 134-149, 145-158 and 159-164. The labile disulphide bond responsible for the enzymatic properties of the sweet tasting protein thaumatin appeared to be between Cys-145 and Cys-158. |
| format | Article |
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The peptides obtained after proteolytic cleavage with trypsin and pepsin, and in one case with chymotrypsin have been purified by gel filtration, high-performance liquid chromatography and peptide mapping by paper high-voltage electrophoresis in one direction and paper chromatography in the second dimension. Disulphide bonds appeared to be formed by cysteine residues in positions 9-204, 56-66, 71-77, 121-193, 126-177, 134-149, 145-158 and 159-164. The labile disulphide bond responsible for the enzymatic properties of the sweet tasting protein thaumatin appeared to be between Cys-145 and Cys-158.</description><identifier>ISSN: 0014-2956</identifier><language>eng</language><subject>cysteine ; disulfide bonds ; electrophoresis ; pepsin ; peptide mapping ; sweetness ; thaumatin ; trypsin</subject><ispartof>European journal of biochemistry, 1984-01, Vol.144 (1), p.41-45</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>Van Der Wel, H</creatorcontrib><creatorcontrib>Iyengar, R B</creatorcontrib><creatorcontrib>Van Brouwershaven, J</creatorcontrib><creatorcontrib>Van Wassenaar, PD</creatorcontrib><creatorcontrib>Bel, W J</creatorcontrib><creatorcontrib>Van Der Ouderaa, FJG</creatorcontrib><title>Assignments of the disulphide bonds in the sweet-tasting protein thaumatin I</title><title>European journal of biochemistry</title><description>The disulphide linkages of the 16 half-cyteine residues in the sweet-tasting protein thaumatin have been investigated by enzymatic hydrolysis of the intact molecule. The peptides obtained after proteolytic cleavage with trypsin and pepsin, and in one case with chymotrypsin have been purified by gel filtration, high-performance liquid chromatography and peptide mapping by paper high-voltage electrophoresis in one direction and paper chromatography in the second dimension. Disulphide bonds appeared to be formed by cysteine residues in positions 9-204, 56-66, 71-77, 121-193, 126-177, 134-149, 145-158 and 159-164. The labile disulphide bond responsible for the enzymatic properties of the sweet tasting protein thaumatin appeared to be between Cys-145 and Cys-158.</description><subject>cysteine</subject><subject>disulfide bonds</subject><subject>electrophoresis</subject><subject>pepsin</subject><subject>peptide mapping</subject><subject>sweetness</subject><subject>thaumatin</subject><subject>trypsin</subject><issn>0014-2956</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1984</creationdate><recordtype>article</recordtype><recordid>eNqNissKwjAQAHNQsD7-YU_eCqk2LT2KKAoevZfUbttImlR3g79vKX6Ap4GZmYlIyiSNd4XKFmJJ9JRSZkWWR-J2IDKt69ExgW-AO4TaULBDZ2qEyruawLjJ0weRY9bExrUwvD3jVHTo9ajguhbzRlvCzY8rsT2f7sdLPL6vgMRlb-iB1mqHPlCZpDJPlFL7v8cvsA5AaQ</recordid><startdate>19840101</startdate><enddate>19840101</enddate><creator>Van Der Wel, H</creator><creator>Iyengar, R B</creator><creator>Van Brouwershaven, J</creator><creator>Van Wassenaar, PD</creator><creator>Bel, W J</creator><creator>Van Der Ouderaa, FJG</creator><scope>7QL</scope><scope>7QR</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>19840101</creationdate><title>Assignments of the disulphide bonds in the sweet-tasting protein thaumatin I</title><author>Van Der Wel, H ; Iyengar, R B ; Van Brouwershaven, J ; Van Wassenaar, PD ; Bel, W J ; Van Der Ouderaa, FJG</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_miscellaneous_140715553</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1984</creationdate><topic>cysteine</topic><topic>disulfide bonds</topic><topic>electrophoresis</topic><topic>pepsin</topic><topic>peptide mapping</topic><topic>sweetness</topic><topic>thaumatin</topic><topic>trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Der Wel, H</creatorcontrib><creatorcontrib>Iyengar, R B</creatorcontrib><creatorcontrib>Van Brouwershaven, J</creatorcontrib><creatorcontrib>Van Wassenaar, PD</creatorcontrib><creatorcontrib>Bel, W J</creatorcontrib><creatorcontrib>Van Der Ouderaa, FJG</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Der Wel, H</au><au>Iyengar, R B</au><au>Van Brouwershaven, J</au><au>Van Wassenaar, PD</au><au>Bel, W J</au><au>Van Der Ouderaa, FJG</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Assignments of the disulphide bonds in the sweet-tasting protein thaumatin I</atitle><jtitle>European journal of biochemistry</jtitle><date>1984-01-01</date><risdate>1984</risdate><volume>144</volume><issue>1</issue><spage>41</spage><epage>45</epage><pages>41-45</pages><issn>0014-2956</issn><abstract>The disulphide linkages of the 16 half-cyteine residues in the sweet-tasting protein thaumatin have been investigated by enzymatic hydrolysis of the intact molecule. The peptides obtained after proteolytic cleavage with trypsin and pepsin, and in one case with chymotrypsin have been purified by gel filtration, high-performance liquid chromatography and peptide mapping by paper high-voltage electrophoresis in one direction and paper chromatography in the second dimension. Disulphide bonds appeared to be formed by cysteine residues in positions 9-204, 56-66, 71-77, 121-193, 126-177, 134-149, 145-158 and 159-164. The labile disulphide bond responsible for the enzymatic properties of the sweet tasting protein thaumatin appeared to be between Cys-145 and Cys-158.</abstract></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-2956 |
| ispartof | European journal of biochemistry, 1984-01, Vol.144 (1), p.41-45 |
| issn | 0014-2956 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_14071555 |
| source | Alma/SFX Local Collection |
| subjects | cysteine disulfide bonds electrophoresis pepsin peptide mapping sweetness thaumatin trypsin |
| title | Assignments of the disulphide bonds in the sweet-tasting protein thaumatin I |
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