Limited heterogeneity of neurosecretory proteins produced by the bag cells of Aplysia
The heterogeneity of the low-molecular-weight (≤11,000 daltons) protein products synthesized by the bag cells of Aplysia in the presence of labeled amino acids was assessed by sequential sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing. The bag cells synt...
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Veröffentlicht in: | General and comparative endocrinology 1981-01, Vol.43 (3), p.308-314 |
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description | The heterogeneity of the low-molecular-weight (≤11,000 daltons) protein products synthesized by the bag cells of
Aplysia in the presence of labeled amino acids was assessed by sequential sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing. The bag cells synthesize two major low-molecular-weight products: an acidic (p
I 4.9) peptide with an apparent molecular weight of 4500 daltons, and a basic (p
I 9.6) peptide that migrates at an apparent molecular weight of 1500 daltons in our SDS-PAGE system. In addition, a p
I 8.2 peptide comigrates with the major basic product on SDS-PAGE, but comprises less than 20% of the labeled material in this region of the gels. The major basic product must be egg laying hormone, a basic (p
I 9.3–9.7) peptide that is a known product of these cells. Since egg laying hormone has a molecular weight of 4385 daltons as calculated from its amino acid composition, it appears to migrate anomalously on SDS-PAGE. The apparent molecular-weight heterogeneity of bag cell products previously reported by other investigators can thus be attributed to the anomalous behavior of egg laying hormone in some SDS-PAGE systems. |
doi_str_mv | 10.1016/0016-6480(81)90289-6 |
format | Article |
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Aplysia in the presence of labeled amino acids was assessed by sequential sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing. The bag cells synthesize two major low-molecular-weight products: an acidic (p
I 4.9) peptide with an apparent molecular weight of 4500 daltons, and a basic (p
I 9.6) peptide that migrates at an apparent molecular weight of 1500 daltons in our SDS-PAGE system. In addition, a p
I 8.2 peptide comigrates with the major basic product on SDS-PAGE, but comprises less than 20% of the labeled material in this region of the gels. The major basic product must be egg laying hormone, a basic (p
I 9.3–9.7) peptide that is a known product of these cells. Since egg laying hormone has a molecular weight of 4385 daltons as calculated from its amino acid composition, it appears to migrate anomalously on SDS-PAGE. The apparent molecular-weight heterogeneity of bag cell products previously reported by other investigators can thus be attributed to the anomalous behavior of egg laying hormone in some SDS-PAGE systems.</description><identifier>ISSN: 0016-6480</identifier><identifier>EISSN: 1095-6840</identifier><identifier>DOI: 10.1016/0016-6480(81)90289-6</identifier><identifier>PMID: 7215781</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Aplysia ; Aplysia - analysis ; Electrophoresis, Polyacrylamide Gel ; Invertebrate Hormones - isolation & purification ; Isoelectric Focusing ; Nerve Tissue Proteins - isolation & purification ; Neurosecretory Systems - analysis</subject><ispartof>General and comparative endocrinology, 1981-01, Vol.43 (3), p.308-314</ispartof><rights>1981</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c388t-39a3240029de621c974a73d33b39d50e8cc3e11778499cb0b1ceea24c86f154f3</citedby><cites>FETCH-LOGICAL-c388t-39a3240029de621c974a73d33b39d50e8cc3e11778499cb0b1ceea24c86f154f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0016-6480(81)90289-6$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,777,781,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7215781$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yates, Michael E.</creatorcontrib><creatorcontrib>Berry, Robert W.</creatorcontrib><title>Limited heterogeneity of neurosecretory proteins produced by the bag cells of Aplysia</title><title>General and comparative endocrinology</title><addtitle>Gen Comp Endocrinol</addtitle><description>The heterogeneity of the low-molecular-weight (≤11,000 daltons) protein products synthesized by the bag cells of
Aplysia in the presence of labeled amino acids was assessed by sequential sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing. The bag cells synthesize two major low-molecular-weight products: an acidic (p
I 4.9) peptide with an apparent molecular weight of 4500 daltons, and a basic (p
I 9.6) peptide that migrates at an apparent molecular weight of 1500 daltons in our SDS-PAGE system. In addition, a p
I 8.2 peptide comigrates with the major basic product on SDS-PAGE, but comprises less than 20% of the labeled material in this region of the gels. The major basic product must be egg laying hormone, a basic (p
I 9.3–9.7) peptide that is a known product of these cells. Since egg laying hormone has a molecular weight of 4385 daltons as calculated from its amino acid composition, it appears to migrate anomalously on SDS-PAGE. The apparent molecular-weight heterogeneity of bag cell products previously reported by other investigators can thus be attributed to the anomalous behavior of egg laying hormone in some SDS-PAGE systems.</description><subject>Animals</subject><subject>Aplysia</subject><subject>Aplysia - analysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Invertebrate Hormones - isolation & purification</subject><subject>Isoelectric Focusing</subject><subject>Nerve Tissue Proteins - isolation & purification</subject><subject>Neurosecretory Systems - analysis</subject><issn>0016-6480</issn><issn>1095-6840</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLxDAQx4Mouj6-gUJPoofqpGnzuAiL-IIFL3oObTrdjXTbNUmFfntTd_Gol5mB-f_n8SPknMINBcpvIYaU5xKuJL1WkEmV8j0yo6CKlMsc9snsV3JEjr3_AICCcXpIDkVGCyHpjLwv7NoGrJMVBnT9Eju0YUz6JulwcL1H4zD0bkw2rg9oOz8V9WCioxqTsMKkKpeJwbb1k2m-aUdvy1Ny0JStx7NdPiHvjw9v98_p4vXp5X6-SA2TMqRMlSzLATJVI8-oUSIvBasZq5iqC0BpDENKhZC5UqaCihrEMsuN5A0t8oadkMvt3HjU54A-6LX10zFlh_3gtSg4gCzUv0JaZEIpwaIw3wpNfN47bPTG2XXpRk1BT9j1xFRPTLWk-ge75tF2sZs_VGusf007zrF_t-1jpPFl0WlvLHYRo3Vogq57-_eCb3VhkW4</recordid><startdate>19810101</startdate><enddate>19810101</enddate><creator>Yates, Michael E.</creator><creator>Berry, Robert W.</creator><general>Elsevier Inc</general><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>F1W</scope><scope>H95</scope><scope>L.G</scope><scope>7X8</scope></search><sort><creationdate>19810101</creationdate><title>Limited heterogeneity of neurosecretory proteins produced by the bag cells of Aplysia</title><author>Yates, Michael E. ; Berry, Robert W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-39a3240029de621c974a73d33b39d50e8cc3e11778499cb0b1ceea24c86f154f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Animals</topic><topic>Aplysia</topic><topic>Aplysia - analysis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Invertebrate Hormones - isolation & purification</topic><topic>Isoelectric Focusing</topic><topic>Nerve Tissue Proteins - isolation & purification</topic><topic>Neurosecretory Systems - analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yates, Michael E.</creatorcontrib><creatorcontrib>Berry, Robert W.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><jtitle>General and comparative endocrinology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yates, Michael E.</au><au>Berry, Robert W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Limited heterogeneity of neurosecretory proteins produced by the bag cells of Aplysia</atitle><jtitle>General and comparative endocrinology</jtitle><addtitle>Gen Comp Endocrinol</addtitle><date>1981-01-01</date><risdate>1981</risdate><volume>43</volume><issue>3</issue><spage>308</spage><epage>314</epage><pages>308-314</pages><issn>0016-6480</issn><eissn>1095-6840</eissn><abstract>The heterogeneity of the low-molecular-weight (≤11,000 daltons) protein products synthesized by the bag cells of
Aplysia in the presence of labeled amino acids was assessed by sequential sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and isoelectric focusing. The bag cells synthesize two major low-molecular-weight products: an acidic (p
I 4.9) peptide with an apparent molecular weight of 4500 daltons, and a basic (p
I 9.6) peptide that migrates at an apparent molecular weight of 1500 daltons in our SDS-PAGE system. In addition, a p
I 8.2 peptide comigrates with the major basic product on SDS-PAGE, but comprises less than 20% of the labeled material in this region of the gels. The major basic product must be egg laying hormone, a basic (p
I 9.3–9.7) peptide that is a known product of these cells. Since egg laying hormone has a molecular weight of 4385 daltons as calculated from its amino acid composition, it appears to migrate anomalously on SDS-PAGE. The apparent molecular-weight heterogeneity of bag cell products previously reported by other investigators can thus be attributed to the anomalous behavior of egg laying hormone in some SDS-PAGE systems.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7215781</pmid><doi>10.1016/0016-6480(81)90289-6</doi><tpages>7</tpages></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals |
subjects | Animals Aplysia Aplysia - analysis Electrophoresis, Polyacrylamide Gel Invertebrate Hormones - isolation & purification Isoelectric Focusing Nerve Tissue Proteins - isolation & purification Neurosecretory Systems - analysis |
title | Limited heterogeneity of neurosecretory proteins produced by the bag cells of Aplysia |
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