IMMUNOCHEMICAL IDENTIFICATION OF NEUTRAL PEPTIDE HYDROLASES IN DORMANT AND GERMINATING BARLEY GRAINS
The chromogenic substrate, N‐acetyl‐DL‐phenylalanine‐β‐naphthyl ester (APNE), used in trypsin or chymotrypsin studies, has been employed to identify neutral peptide hydrolases in barley by immunoelectrophoretic analysis. Enzyme activity was observed in proximal (embryo part) and distal (endosperm pa...
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| Veröffentlicht in: | International Journal of Peptide and Protein Research 1974-01, Vol.6 (1), p.13-19 |
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| container_title | International Journal of Peptide and Protein Research |
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| creator | Tronier, Bente Ory, Robert L. Djurtoft, Robert J. |
| description | The chromogenic substrate, N‐acetyl‐DL‐phenylalanine‐β‐naphthyl ester (APNE), used in trypsin or chymotrypsin studies, has been employed to identify neutral peptide hydrolases in barley by immunoelectrophoretic analysis. Enzyme activity was observed in proximal (embryo part) and distal (endosperm part) portions of barley grains before and after germination. The proximal portion contained all detectable activity in the ungerminated seed. This enzyme migrates strongly towards the anode. During germination a new enzyme is formed which hydrolyzes the same substrate but is electrophoretically different from the enzyme found in dormant grains (it is more neutral or cathodic). The newly‐formed enzyme appears in the proximal part of the seed after 34 hours of germination and in the distal part after 96 hours. This enzyme does not appear to be a carboxypeptidase but may be related to one (or more) of the reported barley aminopeptidases. |
| doi_str_mv | 10.1111/j.1399-3011.1974.tb02353.x |
| format | Article |
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Enzyme activity was observed in proximal (embryo part) and distal (endosperm part) portions of barley grains before and after germination. The proximal portion contained all detectable activity in the ungerminated seed. This enzyme migrates strongly towards the anode. During germination a new enzyme is formed which hydrolyzes the same substrate but is electrophoretically different from the enzyme found in dormant grains (it is more neutral or cathodic). The newly‐formed enzyme appears in the proximal part of the seed after 34 hours of germination and in the distal part after 96 hours. This enzyme does not appear to be a carboxypeptidase but may be related to one (or more) of the reported barley aminopeptidases.</description><identifier>ISSN: 0367-8377</identifier><identifier>EISSN: 1399-3011</identifier><identifier>DOI: 10.1111/j.1399-3011.1974.tb02353.x</identifier><identifier>PMID: 4859357</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Antibodies ; Antigens ; Carboxypeptidases - analysis ; Edible Grain - enzymology ; Esters ; Hydrolysis ; Immune Sera ; Immunoelectrophoresis ; Methods ; Peptide Hydrolases - analysis ; Phenylalanine ; Rabbits - immunology ; Time Factors</subject><ispartof>International Journal of Peptide and Protein Research, 1974-01, Vol.6 (1), p.13-19</ispartof><rights>1974 Munksgaard International Publishers Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3503-7eb491f5180d2abe1fc0dc9525fc6c577c32d203aa1710e339a7594ac16dab7f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1399-3011.1974.tb02353.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1399-3011.1974.tb02353.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,4009,27902,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4859357$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tronier, Bente</creatorcontrib><creatorcontrib>Ory, Robert L.</creatorcontrib><creatorcontrib>Djurtoft, Robert J.</creatorcontrib><title>IMMUNOCHEMICAL IDENTIFICATION OF NEUTRAL PEPTIDE HYDROLASES IN DORMANT AND GERMINATING BARLEY GRAINS</title><title>International Journal of Peptide and Protein Research</title><addtitle>Int J Pept Protein Res</addtitle><description>The chromogenic substrate, N‐acetyl‐DL‐phenylalanine‐β‐naphthyl ester (APNE), used in trypsin or chymotrypsin studies, has been employed to identify neutral peptide hydrolases in barley by immunoelectrophoretic analysis. Enzyme activity was observed in proximal (embryo part) and distal (endosperm part) portions of barley grains before and after germination. The proximal portion contained all detectable activity in the ungerminated seed. This enzyme migrates strongly towards the anode. During germination a new enzyme is formed which hydrolyzes the same substrate but is electrophoretically different from the enzyme found in dormant grains (it is more neutral or cathodic). The newly‐formed enzyme appears in the proximal part of the seed after 34 hours of germination and in the distal part after 96 hours. This enzyme does not appear to be a carboxypeptidase but may be related to one (or more) of the reported barley aminopeptidases.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antigens</subject><subject>Carboxypeptidases - analysis</subject><subject>Edible Grain - enzymology</subject><subject>Esters</subject><subject>Hydrolysis</subject><subject>Immune Sera</subject><subject>Immunoelectrophoresis</subject><subject>Methods</subject><subject>Peptide Hydrolases - analysis</subject><subject>Phenylalanine</subject><subject>Rabbits - immunology</subject><subject>Time Factors</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1974</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkNFumzAUhq1qVZe1fYRJ1i52B7M5GIddTKKBEKZgWkI29coyxkjJkqbDiZa-fUGJcj_fHEvf-f8jfQh9ocSl_fu2dimEoQOEUpeG3Hf3NfGAgXu8QqML-oBGBALujIHzj-iTtWtCwAfu3aAbf8xCYHyEmizPl6KYzJI8m0RznMWJqLJp_6-yQuBiikWyrMqePCaPVU_x7Dkui3m0SBY4EzguyjwSFY5EjNOkzDPRB0WKH6JynjzjtIwysbhD163aWHN_nrdoOU2qycyZF-lw1dHACDjc1H5IW0bHpPFUbWirSaND5rFWB5pxrsFrPAJKUU6JAQgVZ6GvNA0aVfMWbtHXU-9rt_t7MHYvtyurzWajXszuYOXY83ngU69f_H5a1N3O2s608rVbbVX3JimRg2K5loNHOXiUg2J5ViyPffjz-cqh3prmEj077fmPE_-32pi3_2iWk4c4ptAXOKeCld2b46VAdX9kwIEz-Vuk8tfPJ0qZKCWDdyTKkgQ</recordid><startdate>197401</startdate><enddate>197401</enddate><creator>Tronier, Bente</creator><creator>Ory, Robert L.</creator><creator>Djurtoft, Robert J.</creator><general>Blackwell Publishing Ltd</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>7X8</scope></search><sort><creationdate>197401</creationdate><title>IMMUNOCHEMICAL IDENTIFICATION OF NEUTRAL PEPTIDE HYDROLASES IN DORMANT AND GERMINATING BARLEY GRAINS</title><author>Tronier, Bente ; Ory, Robert L. ; Djurtoft, Robert J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3503-7eb491f5180d2abe1fc0dc9525fc6c577c32d203aa1710e339a7594ac16dab7f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1974</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antigens</topic><topic>Carboxypeptidases - analysis</topic><topic>Edible Grain - enzymology</topic><topic>Esters</topic><topic>Hydrolysis</topic><topic>Immune Sera</topic><topic>Immunoelectrophoresis</topic><topic>Methods</topic><topic>Peptide Hydrolases - analysis</topic><topic>Phenylalanine</topic><topic>Rabbits - immunology</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tronier, Bente</creatorcontrib><creatorcontrib>Ory, Robert L.</creatorcontrib><creatorcontrib>Djurtoft, Robert J.</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>MEDLINE - Academic</collection><jtitle>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tronier, Bente</au><au>Ory, Robert L.</au><au>Djurtoft, Robert J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>IMMUNOCHEMICAL IDENTIFICATION OF NEUTRAL PEPTIDE HYDROLASES IN DORMANT AND GERMINATING BARLEY GRAINS</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><addtitle>Int J Pept Protein Res</addtitle><date>1974-01</date><risdate>1974</risdate><volume>6</volume><issue>1</issue><spage>13</spage><epage>19</epage><pages>13-19</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><abstract>The chromogenic substrate, N‐acetyl‐DL‐phenylalanine‐β‐naphthyl ester (APNE), used in trypsin or chymotrypsin studies, has been employed to identify neutral peptide hydrolases in barley by immunoelectrophoretic analysis. Enzyme activity was observed in proximal (embryo part) and distal (endosperm part) portions of barley grains before and after germination. The proximal portion contained all detectable activity in the ungerminated seed. This enzyme migrates strongly towards the anode. During germination a new enzyme is formed which hydrolyzes the same substrate but is electrophoretically different from the enzyme found in dormant grains (it is more neutral or cathodic). The newly‐formed enzyme appears in the proximal part of the seed after 34 hours of germination and in the distal part after 96 hours. This enzyme does not appear to be a carboxypeptidase but may be related to one (or more) of the reported barley aminopeptidases.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>4859357</pmid><doi>10.1111/j.1399-3011.1974.tb02353.x</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0367-8377 |
| ispartof | International Journal of Peptide and Protein Research, 1974-01, Vol.6 (1), p.13-19 |
| issn | 0367-8377 1399-3011 |
| language | eng |
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| source | MEDLINE; Wiley Online Library |
| subjects | Animals Antibodies Antigens Carboxypeptidases - analysis Edible Grain - enzymology Esters Hydrolysis Immune Sera Immunoelectrophoresis Methods Peptide Hydrolases - analysis Phenylalanine Rabbits - immunology Time Factors |
| title | IMMUNOCHEMICAL IDENTIFICATION OF NEUTRAL PEPTIDE HYDROLASES IN DORMANT AND GERMINATING BARLEY GRAINS |
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