Characterization of the proteins from melanoplus bivittatus that bind juvenile hormone, and a refined efda photolabeling technique
1. 1. Juvenile hormone (JH) is specifically bound by a protein from hemolymph and fat body cytosol of the grasshopper, Melanoplus bivittatus. 2. 2. This protein has a native molecular weight of 331,000 and subunits of 77,000. 3. 3. Proteins that bind JH were covalently photolabeled with a JH analog,...
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| Veröffentlicht in: | International journal of biochemistry 1992-09, Vol.24 (9), p.1435-1446 |
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| container_issue | 9 |
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| container_title | International journal of biochemistry |
| container_volume | 24 |
| creator | Winder, Bruce S. Roberts, P.Elaine |
| description | 1.
1. Juvenile hormone (JH) is specifically bound by a protein from hemolymph and fat body cytosol of the grasshopper,
Melanoplus bivittatus.
2.
2. This protein has a native molecular weight of 331,000 and subunits of 77,000.
3.
3. Proteins that bind JH were covalently photolabeled with a JH analog, epoxyfarnesyl diazoacetate (EFDA). Samples were irradiated in spot plates and hydroxyapatite was used to separate bound from free [
3H]EFDA. Differential solubilization was used to extract unlinked [
3H]EFDA and solubilize [
3H]EFDA linked to protein.
4.
4. Hemolymph proteins of
M
r, 479,000, 240,000 and 77,000 also bound [
2+H]EFDA.
5.
5. Proteins that bound [
3,H]EFDA were not vitellogenins. |
| doi_str_mv | 10.1016/0020-711X(92)90069-D |
| format | Article |
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1. Juvenile hormone (JH) is specifically bound by a protein from hemolymph and fat body cytosol of the grasshopper,
Melanoplus bivittatus.
2.
2. This protein has a native molecular weight of 331,000 and subunits of 77,000.
3.
3. Proteins that bind JH were covalently photolabeled with a JH analog, epoxyfarnesyl diazoacetate (EFDA). Samples were irradiated in spot plates and hydroxyapatite was used to separate bound from free [
3H]EFDA. Differential solubilization was used to extract unlinked [
3H]EFDA and solubilize [
3H]EFDA linked to protein.
4.
4. Hemolymph proteins of
M
r, 479,000, 240,000 and 77,000 also bound [
2+H]EFDA.
5.
5. Proteins that bound [
3,H]EFDA were not vitellogenins.</description><identifier>ISSN: 0020-711X</identifier><identifier>DOI: 10.1016/0020-711X(92)90069-D</identifier><identifier>PMID: 1426524</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Affinity Labels ; Animals ; binding proteins ; Carrier Proteins - metabolism ; chemical analysis ; Diazonium Compounds ; Electrophoresis, Gel, Two-Dimensional ; Farnesol - analogs & derivatives ; fat body ; Female ; Grasshoppers - chemistry ; hemolymph ; Insect Proteins ; juvenile hormones ; Juvenile Hormones - metabolism ; Melanoplus bivittatus ; molecular weight</subject><ispartof>International journal of biochemistry, 1992-09, Vol.24 (9), p.1435-1446</ispartof><rights>1992</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-534b062d7bf2c4f28e2b46b8769af9961ed6b98e691a12afdc5d3158673253413</citedby><cites>FETCH-LOGICAL-c381t-534b062d7bf2c4f28e2b46b8769af9961ed6b98e691a12afdc5d3158673253413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1426524$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Winder, Bruce S.</creatorcontrib><creatorcontrib>Roberts, P.Elaine</creatorcontrib><title>Characterization of the proteins from melanoplus bivittatus that bind juvenile hormone, and a refined efda photolabeling technique</title><title>International journal of biochemistry</title><addtitle>Int J Biochem</addtitle><description>1.
1. Juvenile hormone (JH) is specifically bound by a protein from hemolymph and fat body cytosol of the grasshopper,
Melanoplus bivittatus.
2.
2. This protein has a native molecular weight of 331,000 and subunits of 77,000.
3.
3. Proteins that bind JH were covalently photolabeled with a JH analog, epoxyfarnesyl diazoacetate (EFDA). Samples were irradiated in spot plates and hydroxyapatite was used to separate bound from free [
3H]EFDA. Differential solubilization was used to extract unlinked [
3H]EFDA and solubilize [
3H]EFDA linked to protein.
4.
4. Hemolymph proteins of
M
r, 479,000, 240,000 and 77,000 also bound [
2+H]EFDA.
5.
5. Proteins that bound [
3,H]EFDA were not vitellogenins.</description><subject>Affinity Labels</subject><subject>Animals</subject><subject>binding proteins</subject><subject>Carrier Proteins - metabolism</subject><subject>chemical analysis</subject><subject>Diazonium Compounds</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Farnesol - analogs & derivatives</subject><subject>fat body</subject><subject>Female</subject><subject>Grasshoppers - chemistry</subject><subject>hemolymph</subject><subject>Insect Proteins</subject><subject>juvenile hormones</subject><subject>Juvenile Hormones - metabolism</subject><subject>Melanoplus bivittatus</subject><subject>molecular weight</subject><issn>0020-711X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9vFSEUxVloaq1-A42sjE2cCgyPGTZNzKt_mjRxoU3cEQYuHZoZeALzEl32k8tzmnbnCrj3nHs5P4ReUXJGCRUfCGGk6Sj9-U6yU0mIkM3FE3T8UH6Gnud8SwiVPadH6IhyJjaMH6O77aiTNgWS_6OLjwFHh8sIeJdiAR8ydinOeIZJh7iblowHv_el6FKvZdSlvoPFt8segp8AjzHNMcB7rGtV4wTOB7AYnNV4N8YSJz3A5MMNLmDG4H8t8AI9dXrK8PL-PEHXnz_92H5trr59udx-vGpM29PSbFo-EMFsNzhmuGM9sIGLoe-E1E5KQcGKQfYgJNWUaWfNxrZ004uuZdVL2xP0dp1bo9W1uajZZwNTTQZxyarqOkl5V4V8FZoUc64R1C75WaffihJ1wK0OXNWBq5JM_cOtLqrt9f38ZZjBPppW1rX_Zu07HZW-ST6r6--M0JbQTjDGWVWcrwqoGPYeksrGQzBgfQJTlI3-_1_4C_3knN0</recordid><startdate>19920901</startdate><enddate>19920901</enddate><creator>Winder, Bruce S.</creator><creator>Roberts, P.Elaine</creator><general>Elsevier B.V</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>19920901</creationdate><title>Characterization of the proteins from melanoplus bivittatus that bind juvenile hormone, and a refined efda photolabeling technique</title><author>Winder, Bruce S. ; Roberts, P.Elaine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-534b062d7bf2c4f28e2b46b8769af9961ed6b98e691a12afdc5d3158673253413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Affinity Labels</topic><topic>Animals</topic><topic>binding proteins</topic><topic>Carrier Proteins - metabolism</topic><topic>chemical analysis</topic><topic>Diazonium Compounds</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Farnesol - analogs & derivatives</topic><topic>fat body</topic><topic>Female</topic><topic>Grasshoppers - chemistry</topic><topic>hemolymph</topic><topic>Insect Proteins</topic><topic>juvenile hormones</topic><topic>Juvenile Hormones - metabolism</topic><topic>Melanoplus bivittatus</topic><topic>molecular weight</topic><toplevel>online_resources</toplevel><creatorcontrib>Winder, Bruce S.</creatorcontrib><creatorcontrib>Roberts, P.Elaine</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>International journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Winder, Bruce S.</au><au>Roberts, P.Elaine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the proteins from melanoplus bivittatus that bind juvenile hormone, and a refined efda photolabeling technique</atitle><jtitle>International journal of biochemistry</jtitle><addtitle>Int J Biochem</addtitle><date>1992-09-01</date><risdate>1992</risdate><volume>24</volume><issue>9</issue><spage>1435</spage><epage>1446</epage><pages>1435-1446</pages><issn>0020-711X</issn><abstract>1.
1. Juvenile hormone (JH) is specifically bound by a protein from hemolymph and fat body cytosol of the grasshopper,
Melanoplus bivittatus.
2.
2. This protein has a native molecular weight of 331,000 and subunits of 77,000.
3.
3. Proteins that bind JH were covalently photolabeled with a JH analog, epoxyfarnesyl diazoacetate (EFDA). Samples were irradiated in spot plates and hydroxyapatite was used to separate bound from free [
3H]EFDA. Differential solubilization was used to extract unlinked [
3H]EFDA and solubilize [
3H]EFDA linked to protein.
4.
4. Hemolymph proteins of
M
r, 479,000, 240,000 and 77,000 also bound [
2+H]EFDA.
5.
5. Proteins that bound [
3,H]EFDA were not vitellogenins.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>1426524</pmid><doi>10.1016/0020-711X(92)90069-D</doi><tpages>12</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | International journal of biochemistry, 1992-09, Vol.24 (9), p.1435-1446 |
| issn | 0020-711X |
| language | eng |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Affinity Labels Animals binding proteins Carrier Proteins - metabolism chemical analysis Diazonium Compounds Electrophoresis, Gel, Two-Dimensional Farnesol - analogs & derivatives fat body Female Grasshoppers - chemistry hemolymph Insect Proteins juvenile hormones Juvenile Hormones - metabolism Melanoplus bivittatus molecular weight |
| title | Characterization of the proteins from melanoplus bivittatus that bind juvenile hormone, and a refined efda photolabeling technique |
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