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Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)
Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting pr...
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Published in: | Journal of experimental botany 1999-01, Vol.50 (330), p.63-69 |
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creator | Omarov, Rustem T. Akaba, Shuichi Koshiba, Tomokazu Lips, S. Herman |
description | Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting proteins were detected in barley plants capable of oxidizing a number of aliphatic and aromatic aldehydes such as indole-3-aldehyde, acetaldehyde, heptaldehyde, and benzaldehyde. Mouse polyclonal antibodies raised against purified maize AO cross-reacted with barley AO proteins extracted from roots, leaves and seeds. At least three different AO proteins were detected in roots on the basis of their mobility during PAGE after native Western blot analysis while in leaves and seeds only one polypeptide cross-reacted with the antibody. SDS-immunoblot analysis showed marked differences in molecular weight between subunits of the AO bands extracted from roots, leaves and seeds. Two distinct subunit bands were observed in roots, with relatively close molecular weights (160 kDa and 145 kDa), while a single subunit with a molecular weight of 150 kDa was observed in leaf and seed extracts. Menadione, a specific and potent inhibitor of animal AO did not affect barley AO proteins. Root and leaf AO differed in their thermostability and susceptibility to exogenous tungstate. The AO proteins in plants may be a group of enzymes with different substrate specificity, tissue distribution and presumably fulfilling different metabolic roles in each plant organ. |
doi_str_mv | 10.1093/jxb/50.330.63 |
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Herman</creator><creatorcontrib>Omarov, Rustem T. ; Akaba, Shuichi ; Koshiba, Tomokazu ; Lips, S. Herman</creatorcontrib><description>Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting proteins were detected in barley plants capable of oxidizing a number of aliphatic and aromatic aldehydes such as indole-3-aldehyde, acetaldehyde, heptaldehyde, and benzaldehyde. Mouse polyclonal antibodies raised against purified maize AO cross-reacted with barley AO proteins extracted from roots, leaves and seeds. At least three different AO proteins were detected in roots on the basis of their mobility during PAGE after native Western blot analysis while in leaves and seeds only one polypeptide cross-reacted with the antibody. SDS-immunoblot analysis showed marked differences in molecular weight between subunits of the AO bands extracted from roots, leaves and seeds. Two distinct subunit bands were observed in roots, with relatively close molecular weights (160 kDa and 145 kDa), while a single subunit with a molecular weight of 150 kDa was observed in leaf and seed extracts. Menadione, a specific and potent inhibitor of animal AO did not affect barley AO proteins. Root and leaf AO differed in their thermostability and susceptibility to exogenous tungstate. The AO proteins in plants may be a group of enzymes with different substrate specificity, tissue distribution and presumably fulfilling different metabolic roles in each plant organ.</description><identifier>ISSN: 0022-0957</identifier><identifier>EISSN: 1460-2431</identifier><identifier>DOI: 10.1093/jxb/50.330.63</identifier><identifier>CODEN: JEBOA6</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Aldehyde oxidase ; Aldehydes ; Barley ; Biological and medical sciences ; Cell and Molecular Biology, Biochemistry and Molecular Physiology ; Enzymes ; Fundamental and applied biological sciences. 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Herman</creatorcontrib><title>Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)</title><title>Journal of experimental botany</title><addtitle>Journal of Experimental Botany</addtitle><description>Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting proteins were detected in barley plants capable of oxidizing a number of aliphatic and aromatic aldehydes such as indole-3-aldehyde, acetaldehyde, heptaldehyde, and benzaldehyde. Mouse polyclonal antibodies raised against purified maize AO cross-reacted with barley AO proteins extracted from roots, leaves and seeds. At least three different AO proteins were detected in roots on the basis of their mobility during PAGE after native Western blot analysis while in leaves and seeds only one polypeptide cross-reacted with the antibody. SDS-immunoblot analysis showed marked differences in molecular weight between subunits of the AO bands extracted from roots, leaves and seeds. Two distinct subunit bands were observed in roots, with relatively close molecular weights (160 kDa and 145 kDa), while a single subunit with a molecular weight of 150 kDa was observed in leaf and seed extracts. Menadione, a specific and potent inhibitor of animal AO did not affect barley AO proteins. Root and leaf AO differed in their thermostability and susceptibility to exogenous tungstate. The AO proteins in plants may be a group of enzymes with different substrate specificity, tissue distribution and presumably fulfilling different metabolic roles in each plant organ.</description><subject>Aldehyde oxidase</subject><subject>Aldehydes</subject><subject>Barley</subject><subject>Biological and medical sciences</subject><subject>Cell and Molecular Biology, Biochemistry and Molecular Physiology</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Leaves</subject><subject>Metabolism</subject><subject>molybdenum cofactor (MoCo)</subject><subject>Nitrates</subject><subject>Oxidases</subject><subject>Plant physiology</subject><subject>Plant physiology and development</subject><subject>Plant roots</subject><subject>Plants</subject><subject>roots</subject><subject>Seedlings</subject><subject>seeds</subject><subject>Tungstates</subject><issn>0022-0957</issn><issn>1460-2431</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNpFkM1LAzEUxIMoWD-OHoUgHhTc-rJvk3WPRbRVKx78QLyE1-xb3bo2mrTS_veutOhpDvObGRgh9hR0FRR4Op6PTjV0EaFrcE10VGYgSTNU66IDkKYJFDrfFFsxjgFAg9Ydcd1rSn5blCz9vC4psqwnMng_jSeyYfrmKGlSyshcRukrOaLQ8EIeDXwoefYhv2fNKwWWw-7xjtioqIm8u9Jt8Xh58XA-SIZ3_avz3jBxCBqTrCCXsipS5Zwa5SZTxpRqpJwBKrHKiZzWjMUZocYCW4HCkNLAVQWgHG6Lg2XvZ_BfM45TO_azMGknbYq6RXSOLZQsIRd8jIEr-xnqDwoLq8D-vmXbt6wG275lzS9_uCql6KipAk1cHf9DxmAKqsX2l9g4Tn34s1M0hVFo_mfrOOX5n0_h3Zocc20Hzy92eGOeLu_7mb3FH8UhgIE</recordid><startdate>199901</startdate><enddate>199901</enddate><creator>Omarov, Rustem T.</creator><creator>Akaba, Shuichi</creator><creator>Koshiba, Tomokazu</creator><creator>Lips, S. Herman</creator><general>Oxford University Press</general><general>OXFORD UNIVERSITY PRESS</general><general>Oxford Publishing Limited (England)</general><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QP</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>199901</creationdate><title>Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)</title><author>Omarov, Rustem T. ; Akaba, Shuichi ; Koshiba, Tomokazu ; Lips, S. Herman</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3053-49ac2e1921cc1b764166d1b1c60ad3f7aac55e398a353938a3096a150eff001c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Aldehyde oxidase</topic><topic>Aldehydes</topic><topic>Barley</topic><topic>Biological and medical sciences</topic><topic>Cell and Molecular Biology, Biochemistry and Molecular Physiology</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Leaves</topic><topic>Metabolism</topic><topic>molybdenum cofactor (MoCo)</topic><topic>Nitrates</topic><topic>Oxidases</topic><topic>Plant physiology</topic><topic>Plant physiology and development</topic><topic>Plant roots</topic><topic>Plants</topic><topic>roots</topic><topic>Seedlings</topic><topic>seeds</topic><topic>Tungstates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Omarov, Rustem T.</creatorcontrib><creatorcontrib>Akaba, Shuichi</creatorcontrib><creatorcontrib>Koshiba, Tomokazu</creatorcontrib><creatorcontrib>Lips, S. Herman</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Journal of experimental botany</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Omarov, Rustem T.</au><au>Akaba, Shuichi</au><au>Koshiba, Tomokazu</au><au>Lips, S. Herman</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)</atitle><jtitle>Journal of experimental botany</jtitle><addtitle>Journal of Experimental Botany</addtitle><date>1999-01</date><risdate>1999</risdate><volume>50</volume><issue>330</issue><spage>63</spage><epage>69</epage><pages>63-69</pages><issn>0022-0957</issn><eissn>1460-2431</eissn><coden>JEBOA6</coden><abstract>Aldehyde oxidase (AO, EC 1.2.3.1) proteins in leaves, roots and seeds of barley (Hordeum vulgare L.) plants were studied. Differences in substrate specificity and mobility in native PAGE between AO proteins extracted from roots, leaves and seeds have been observed. Four clear bands of AO reacting proteins were detected in barley plants capable of oxidizing a number of aliphatic and aromatic aldehydes such as indole-3-aldehyde, acetaldehyde, heptaldehyde, and benzaldehyde. Mouse polyclonal antibodies raised against purified maize AO cross-reacted with barley AO proteins extracted from roots, leaves and seeds. At least three different AO proteins were detected in roots on the basis of their mobility during PAGE after native Western blot analysis while in leaves and seeds only one polypeptide cross-reacted with the antibody. SDS-immunoblot analysis showed marked differences in molecular weight between subunits of the AO bands extracted from roots, leaves and seeds. Two distinct subunit bands were observed in roots, with relatively close molecular weights (160 kDa and 145 kDa), while a single subunit with a molecular weight of 150 kDa was observed in leaf and seed extracts. Menadione, a specific and potent inhibitor of animal AO did not affect barley AO proteins. Root and leaf AO differed in their thermostability and susceptibility to exogenous tungstate. The AO proteins in plants may be a group of enzymes with different substrate specificity, tissue distribution and presumably fulfilling different metabolic roles in each plant organ.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><doi>10.1093/jxb/50.330.63</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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source | Oxford Journals Online; JSTOR Archival Journals |
subjects | Aldehyde oxidase Aldehydes Barley Biological and medical sciences Cell and Molecular Biology, Biochemistry and Molecular Physiology Enzymes Fundamental and applied biological sciences. Psychology Leaves Metabolism molybdenum cofactor (MoCo) Nitrates Oxidases Plant physiology Plant physiology and development Plant roots Plants roots Seedlings seeds Tungstates |
title | Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.) |
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