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Molecular properties of the enzymic phytohemagglutinin of mung bean
Mung bean seeds possess a tetrameric galactose-binding protein that displays two types of activities: (a) a hemagglutinin activity, and (b) an alpha-galactosidase activity. This protein can be reversibly converted by pH changes from a tetrameric form, which possesses both enzymic and hemagglutinin a...
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| Published in: | The Journal of biological chemistry 1981-07, Vol.256 (14), p.7177-7180 |
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| Main Authors: | , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c402t-c762efc11c4fae01bbd2439c7855238eb7b1bb7ffcf500d4f4fb0841ae3d3b7a3 |
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| cites | cdi_FETCH-LOGICAL-c402t-c762efc11c4fae01bbd2439c7855238eb7b1bb7ffcf500d4f4fb0841ae3d3b7a3 |
| container_end_page | 7180 |
| container_issue | 14 |
| container_start_page | 7177 |
| container_title | The Journal of biological chemistry |
| container_volume | 256 |
| creator | del Campillo, E Shannon, L M Hankins, C N |
| description | Mung bean seeds possess a tetrameric galactose-binding protein that displays two types of activities: (a) a hemagglutinin
activity, and (b) an alpha-galactosidase activity. This protein can be reversibly converted by pH changes from a tetrameric
form, which possesses both enzymic and hemagglutinin activities, to a monomeric form which possesses enzymic activity only.
This observation suggests that the enzymic phytohemagglutinin is an aggregated form of a monomeric alpha-galactosidase. The
tetrameric alpha-galactosidase has a pH optimum of about pH 7.0, while the monomeric form displays a pH optimum of 5.6. Circular
dichroism difference spectra and inhibition studies suggest that aggregation induces conformational changes in the subunits
sufficient to alter their enzymatic properties. The possibility of in vivo changes in subunit equilibria, when combined with
the accompanying alterations in activity, provides a new concept worthy of consideration with respect to the physiological
role of phytohemagglutinins. |
| doi_str_mv | 10.1016/S0021-9258(19)68944-1 |
| format | article |
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activity, and (b) an alpha-galactosidase activity. This protein can be reversibly converted by pH changes from a tetrameric
form, which possesses both enzymic and hemagglutinin activities, to a monomeric form which possesses enzymic activity only.
This observation suggests that the enzymic phytohemagglutinin is an aggregated form of a monomeric alpha-galactosidase. The
tetrameric alpha-galactosidase has a pH optimum of about pH 7.0, while the monomeric form displays a pH optimum of 5.6. Circular
dichroism difference spectra and inhibition studies suggest that aggregation induces conformational changes in the subunits
sufficient to alter their enzymatic properties. The possibility of in vivo changes in subunit equilibria, when combined with
the accompanying alterations in activity, provides a new concept worthy of consideration with respect to the physiological
role of phytohemagglutinins.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)68944-1</identifier><identifier>PMID: 6265439</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>alpha-Galactosidase - metabolism ; Calcium-Binding Proteins ; Carbohydrates ; Carrier Proteins - analysis ; Chemotaxis ; Circular Dichroism ; Galactose - analysis ; Hemagglutination ; Kinetics ; Macromolecular Substances ; Molecular Weight ; Monosaccharide Transport Proteins ; Periplasmic Binding Proteins ; Phytohemagglutinins ; Plant Lectins ; Protein Conformation ; Seeds - enzymology</subject><ispartof>The Journal of biological chemistry, 1981-07, Vol.256 (14), p.7177-7180</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c402t-c762efc11c4fae01bbd2439c7855238eb7b1bb7ffcf500d4f4fb0841ae3d3b7a3</citedby><cites>FETCH-LOGICAL-c402t-c762efc11c4fae01bbd2439c7855238eb7b1bb7ffcf500d4f4fb0841ae3d3b7a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6265439$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>del Campillo, E</creatorcontrib><creatorcontrib>Shannon, L M</creatorcontrib><creatorcontrib>Hankins, C N</creatorcontrib><creatorcontrib>New England Univ., Armidale (Australia)</creatorcontrib><title>Molecular properties of the enzymic phytohemagglutinin of mung bean</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Mung bean seeds possess a tetrameric galactose-binding protein that displays two types of activities: (a) a hemagglutinin
activity, and (b) an alpha-galactosidase activity. This protein can be reversibly converted by pH changes from a tetrameric
form, which possesses both enzymic and hemagglutinin activities, to a monomeric form which possesses enzymic activity only.
This observation suggests that the enzymic phytohemagglutinin is an aggregated form of a monomeric alpha-galactosidase. The
tetrameric alpha-galactosidase has a pH optimum of about pH 7.0, while the monomeric form displays a pH optimum of 5.6. Circular
dichroism difference spectra and inhibition studies suggest that aggregation induces conformational changes in the subunits
sufficient to alter their enzymatic properties. The possibility of in vivo changes in subunit equilibria, when combined with
the accompanying alterations in activity, provides a new concept worthy of consideration with respect to the physiological
role of phytohemagglutinins.</description><subject>alpha-Galactosidase - metabolism</subject><subject>Calcium-Binding Proteins</subject><subject>Carbohydrates</subject><subject>Carrier Proteins - analysis</subject><subject>Chemotaxis</subject><subject>Circular Dichroism</subject><subject>Galactose - analysis</subject><subject>Hemagglutination</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Molecular Weight</subject><subject>Monosaccharide Transport Proteins</subject><subject>Periplasmic Binding Proteins</subject><subject>Phytohemagglutinins</subject><subject>Plant Lectins</subject><subject>Protein Conformation</subject><subject>Seeds - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><recordid>eNo9kEtr3DAQgEVoSTZpfkKCoVDSgxONrId9DEtfkNJDEuhNSNqRreLHVrIp218fbXbJXAZmvhmNPkKugN4CBXn3SCmDsmGivoHms6wbzks4ISugdVVWAn6_I6s35Iycp_SH5uANnJJTyaTgVbMi659Tj27pTSy2cdpinAOmYvLF3GGB4__dEFyx7Xbz1OFg2rZf5jCGcU8My9gWFs34gbz3pk94ecwX5Pnrl6f19_Lh17cf6_uH0nHK5tIpydA7AMe9QQrWbli-walaCFbVaJXNNeW984LSDffcW1pzMFhtKqtMdUE-HfbmS_8umGY9hOSw782I05K0qoSQjDUZFAfQxSmliF5vYxhM3Gmgei9Pv8rTezMaGv0qT0Oeuzo-sNgBN29TR1u5__HQ70Lb_QsRtQ2Ty2I0E1ID1wqUytT1gfJm0qaNIennR2hqRpWUMn_1BSj4gEc</recordid><startdate>19810725</startdate><enddate>19810725</enddate><creator>del Campillo, E</creator><creator>Shannon, L M</creator><creator>Hankins, C N</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>FBQ</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>19810725</creationdate><title>Molecular properties of the enzymic phytohemagglutinin of mung bean</title><author>del Campillo, E ; Shannon, L M ; Hankins, C N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c402t-c762efc11c4fae01bbd2439c7855238eb7b1bb7ffcf500d4f4fb0841ae3d3b7a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>alpha-Galactosidase - metabolism</topic><topic>Calcium-Binding Proteins</topic><topic>Carbohydrates</topic><topic>Carrier Proteins - analysis</topic><topic>Chemotaxis</topic><topic>Circular Dichroism</topic><topic>Galactose - analysis</topic><topic>Hemagglutination</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Molecular Weight</topic><topic>Monosaccharide Transport Proteins</topic><topic>Periplasmic Binding Proteins</topic><topic>Phytohemagglutinins</topic><topic>Plant Lectins</topic><topic>Protein Conformation</topic><topic>Seeds - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>del Campillo, E</creatorcontrib><creatorcontrib>Shannon, L M</creatorcontrib><creatorcontrib>Hankins, C N</creatorcontrib><creatorcontrib>New England Univ., Armidale (Australia)</creatorcontrib><collection>AGRIS</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>del Campillo, E</au><au>Shannon, L M</au><au>Hankins, C N</au><aucorp>New England Univ., Armidale (Australia)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular properties of the enzymic phytohemagglutinin of mung bean</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1981-07-25</date><risdate>1981</risdate><volume>256</volume><issue>14</issue><spage>7177</spage><epage>7180</epage><pages>7177-7180</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Mung bean seeds possess a tetrameric galactose-binding protein that displays two types of activities: (a) a hemagglutinin
activity, and (b) an alpha-galactosidase activity. This protein can be reversibly converted by pH changes from a tetrameric
form, which possesses both enzymic and hemagglutinin activities, to a monomeric form which possesses enzymic activity only.
This observation suggests that the enzymic phytohemagglutinin is an aggregated form of a monomeric alpha-galactosidase. The
tetrameric alpha-galactosidase has a pH optimum of about pH 7.0, while the monomeric form displays a pH optimum of 5.6. Circular
dichroism difference spectra and inhibition studies suggest that aggregation induces conformational changes in the subunits
sufficient to alter their enzymatic properties. The possibility of in vivo changes in subunit equilibria, when combined with
the accompanying alterations in activity, provides a new concept worthy of consideration with respect to the physiological
role of phytohemagglutinins.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>6265439</pmid><doi>10.1016/S0021-9258(19)68944-1</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1981-07, Vol.256 (14), p.7177-7180 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73556229 |
| source | ScienceDirect Journals |
| subjects | alpha-Galactosidase - metabolism Calcium-Binding Proteins Carbohydrates Carrier Proteins - analysis Chemotaxis Circular Dichroism Galactose - analysis Hemagglutination Kinetics Macromolecular Substances Molecular Weight Monosaccharide Transport Proteins Periplasmic Binding Proteins Phytohemagglutinins Plant Lectins Protein Conformation Seeds - enzymology |
| title | Molecular properties of the enzymic phytohemagglutinin of mung bean |
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