Detection of the isoenzymes of wheat grain proteinase a
A new method for the purification of wheat cysteine proteinase A which plays a key role in the mobilization of seed storage proteins during germination has been developed. It consists of (NH 4) 2SO 4 fractionation, gel filtration, and both ion-exchange and hydrophobic chromatography. Constancy of th...
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| Veröffentlicht in: | Phytochemistry (Oxford) 1997-08, Vol.45 (8), p.1549-1553 |
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| creator | Jivotovskaya, Antonina V. Horstmann, Christian Vaintraub, Iosif A. |
| description | A new method for the purification of wheat cysteine proteinase A which plays a key role in the mobilization of seed storage proteins during germination has been developed. It consists of (NH
4)
2SO
4 fractionation, gel filtration, and both ion-exchange and hydrophobic chromatography. Constancy of the specific activity of chromatographic fractions and their SDS-electrophoretic pattern indicates the homogeneity of the final enzyme preparation. However, electrophoresis in nondenaturing conditions revealed three protein bands of similar intensity, each showing proteolytic activity. The N-terminal sequences of all three electrophoretic components are identical. They are also identical to a segment of the amino acid sequence deduced from one of several cDNA clones derived from closely related, but non-identical mRNAs that accumulate in the aleurone layer of gibberellic acid-treated wheat [1]. It is very likely that the three electrophoretic components found are isoenzymes encoded by cDNA clones described by these authors. © 1997 Elsevier Science Ltd. All rights reserved |
| doi_str_mv | 10.1016/S0031-9422(97)00263-X |
| format | Article |
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4)
2SO
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4)
2SO
4 fractionation, gel filtration, and both ion-exchange and hydrophobic chromatography. Constancy of the specific activity of chromatographic fractions and their SDS-electrophoretic pattern indicates the homogeneity of the final enzyme preparation. However, electrophoresis in nondenaturing conditions revealed three protein bands of similar intensity, each showing proteolytic activity. The N-terminal sequences of all three electrophoretic components are identical. They are also identical to a segment of the amino acid sequence deduced from one of several cDNA clones derived from closely related, but non-identical mRNAs that accumulate in the aleurone layer of gibberellic acid-treated wheat [1]. It is very likely that the three electrophoretic components found are isoenzymes encoded by cDNA clones described by these authors. © 1997 Elsevier Science Ltd. All rights reserved</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Aspartic Acid Endopeptidases - chemistry</subject><subject>Aspartic Acid Endopeptidases - genetics</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>cysteine proteinase A</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gramineae</subject><subject>Hydrolases</subject><subject>isenzymes</subject><subject>Isoenzymes - chemistry</subject><subject>Isoenzymes - genetics</subject><subject>Metabolism</subject><subject>Molecular Sequence Data</subject><subject>Plant physiology and development</subject><subject>purification</subject><subject>RNA, Messenger - genetics</subject><subject>seeds</subject><subject>Triticum - enzymology</subject><subject>Triticum aestivum</subject><subject>wheat</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMouq7-hIUeRPRQnSRNpzmJ-A2CBxW8hTSdupHdVpOusv56ux_s1dPAzPPODA9jIw5nHHh-_gwgeaozIU40ngKIXKZvW2zAC5SpRIBtNtgge2w_xg8AUCrPd9muFirTIAcMr6kj1_m2Sdo66caU-NhS8zufUlx0fsZku-Q9WN8kn6HtyDc2UmIP2E5tJ5EO13XIXm9vXq7u08enu4ery8fUyUJ3aWmFAJVJAgSBkhdaVrXVokSpZCkRlbLo8oKjQCWwyhA4z5wsC16oMgM5ZMervf3xrxnFzkx9dDSZ2IbaWTSoeVFkue5BtQJdaGMMVJvP4Kc2zA0HsxBmlsLMwobRaJbCzFufG60PzMopVZvU2lA_P1rPbXR2UgfbOB83mMAMZW98yC5WGPUyvj0FE52nxlHlQ-_XVK3_55E_yB-ElA</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>Jivotovskaya, Antonina V.</creator><creator>Horstmann, Christian</creator><creator>Vaintraub, Iosif A.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</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>7X8</scope></search><sort><creationdate>19970801</creationdate><title>Detection of the isoenzymes of wheat grain proteinase a</title><author>Jivotovskaya, Antonina V. ; Horstmann, Christian ; Vaintraub, Iosif A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c389t-ba220543e0702731893dfa92b7353b37755a7c681727527d470114c3b8185b403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Aspartic Acid Endopeptidases - chemistry</topic><topic>Aspartic Acid Endopeptidases - genetics</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>cysteine proteinase A</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gramineae</topic><topic>Hydrolases</topic><topic>isenzymes</topic><topic>Isoenzymes - chemistry</topic><topic>Isoenzymes - genetics</topic><topic>Metabolism</topic><topic>Molecular Sequence Data</topic><topic>Plant physiology and development</topic><topic>purification</topic><topic>RNA, Messenger - genetics</topic><topic>seeds</topic><topic>Triticum - enzymology</topic><topic>Triticum aestivum</topic><topic>wheat</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jivotovskaya, Antonina V.</creatorcontrib><creatorcontrib>Horstmann, Christian</creatorcontrib><creatorcontrib>Vaintraub, Iosif A.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jivotovskaya, Antonina V.</au><au>Horstmann, Christian</au><au>Vaintraub, Iosif A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Detection of the isoenzymes of wheat grain proteinase a</atitle><jtitle>Phytochemistry (Oxford)</jtitle><addtitle>Phytochemistry</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>45</volume><issue>8</issue><spage>1549</spage><epage>1553</epage><pages>1549-1553</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><abstract>A new method for the purification of wheat cysteine proteinase A which plays a key role in the mobilization of seed storage proteins during germination has been developed. It consists of (NH
4)
2SO
4 fractionation, gel filtration, and both ion-exchange and hydrophobic chromatography. Constancy of the specific activity of chromatographic fractions and their SDS-electrophoretic pattern indicates the homogeneity of the final enzyme preparation. However, electrophoresis in nondenaturing conditions revealed three protein bands of similar intensity, each showing proteolytic activity. The N-terminal sequences of all three electrophoretic components are identical. They are also identical to a segment of the amino acid sequence deduced from one of several cDNA clones derived from closely related, but non-identical mRNAs that accumulate in the aleurone layer of gibberellic acid-treated wheat [1]. It is very likely that the three electrophoretic components found are isoenzymes encoded by cDNA clones described by these authors. © 1997 Elsevier Science Ltd. All rights reserved</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><pmid>9254903</pmid><doi>10.1016/S0031-9422(97)00263-X</doi><tpages>5</tpages></addata></record> |
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| ispartof | Phytochemistry (Oxford), 1997-08, Vol.45 (8), p.1549-1553 |
| issn | 0031-9422 1873-3700 |
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| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Aspartic Acid Endopeptidases - chemistry Aspartic Acid Endopeptidases - genetics Biological and medical sciences Biotechnology cysteine proteinase A Electrophoresis, Polyacrylamide Gel Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gramineae Hydrolases isenzymes Isoenzymes - chemistry Isoenzymes - genetics Metabolism Molecular Sequence Data Plant physiology and development purification RNA, Messenger - genetics seeds Triticum - enzymology Triticum aestivum wheat |
| title | Detection of the isoenzymes of wheat grain proteinase a |
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