Isolation and characterization of hemolymph antifreeze proteins from larvae of the longhorn beetle Rhagium inquisitor (L.)
We describe a simple and effective procedure to isolate antifreeze proteins (AFPs) from the hemolymph of larvae of the longhorn beetle Rhagium inquisitor, and present some characteristics of their structures. Several AFPs were isolated from the hemolymph of this species by heat and acid extraction f...
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| Veröffentlicht in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2005-09, Vol.142 (1), p.90-97 |
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| container_title | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
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| creator | Kristiansen, E. Ramløv, H. Hagen, L. Pedersen, S.A. Andersen, R.A. Zachariassen, K.E. |
| description | We describe a simple and effective procedure to isolate antifreeze proteins (AFPs) from the hemolymph of larvae of the longhorn beetle
Rhagium inquisitor, and present some characteristics of their structures. Several AFPs were isolated from the hemolymph of this species by heat and acid extraction followed by cation exchange. The hemolymph contains at least six AFPs ranging in size from 12.5 to 12.8 kDa. Of these, three were separated to purity by the ion exchange step, as indicated by mass spectrometry. The remaining three forms were further separated by size exclusion chromatography, but could not be isolated to purity. All AFPs in the hemolymph of this species appears to have isoelectric points above 8.00. The dominant form, RiAFP
H4, was purified by the ion exchange step. Its amino acid composition reveals a lower level of cysteine and a higher level of threonine, arginine, alanine and glycine than seen in other insect AFPs. Its trypsin fingerprint does not match that of any known protein. It interacts with ice both in the anionic and cationic state. |
| doi_str_mv | 10.1016/j.cbpc.2005.06.004 |
| format | Article |
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Rhagium inquisitor, and present some characteristics of their structures. Several AFPs were isolated from the hemolymph of this species by heat and acid extraction followed by cation exchange. The hemolymph contains at least six AFPs ranging in size from 12.5 to 12.8 kDa. Of these, three were separated to purity by the ion exchange step, as indicated by mass spectrometry. The remaining three forms were further separated by size exclusion chromatography, but could not be isolated to purity. All AFPs in the hemolymph of this species appears to have isoelectric points above 8.00. The dominant form, RiAFP
H4, was purified by the ion exchange step. Its amino acid composition reveals a lower level of cysteine and a higher level of threonine, arginine, alanine and glycine than seen in other insect AFPs. Its trypsin fingerprint does not match that of any known protein. It interacts with ice both in the anionic and cationic state.</description><identifier>ISSN: 1096-4959</identifier><identifier>EISSN: 1879-1107</identifier><identifier>DOI: 10.1016/j.cbpc.2005.06.004</identifier><identifier>PMID: 15993638</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Alanine - chemistry ; Amino Acids - chemistry ; Amino Acids - metabolism ; Animals ; Antifreeze protein ; Antifreeze Proteins - chemistry ; Antifreeze Proteins - isolation & purification ; Arginine - chemistry ; Beetle ; Cations ; Cerambycidae ; Chromatography, Ion Exchange ; Coleoptera - metabolism ; Cysteine - chemistry ; Glycine - chemistry ; Hemolymph ; Hemolymph - chemistry ; Hemolymph - metabolism ; Insect ; Isoelectric Focusing ; Larva - metabolism ; Mass Spectrometry ; Rhagium inquisitor ; Threonine - chemistry</subject><ispartof>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2005-09, Vol.142 (1), p.90-97</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c385t-d9352aba255a76eb0bdb75bd33da0fea1dee90d45e8e298d493da8c45e5aa06c3</citedby><cites>FETCH-LOGICAL-c385t-d9352aba255a76eb0bdb75bd33da0fea1dee90d45e8e298d493da8c45e5aa06c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1096495905001211$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15993638$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kristiansen, E.</creatorcontrib><creatorcontrib>Ramløv, H.</creatorcontrib><creatorcontrib>Hagen, L.</creatorcontrib><creatorcontrib>Pedersen, S.A.</creatorcontrib><creatorcontrib>Andersen, R.A.</creatorcontrib><creatorcontrib>Zachariassen, K.E.</creatorcontrib><title>Isolation and characterization of hemolymph antifreeze proteins from larvae of the longhorn beetle Rhagium inquisitor (L.)</title><title>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</title><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><description>We describe a simple and effective procedure to isolate antifreeze proteins (AFPs) from the hemolymph of larvae of the longhorn beetle
Rhagium inquisitor, and present some characteristics of their structures. Several AFPs were isolated from the hemolymph of this species by heat and acid extraction followed by cation exchange. The hemolymph contains at least six AFPs ranging in size from 12.5 to 12.8 kDa. Of these, three were separated to purity by the ion exchange step, as indicated by mass spectrometry. The remaining three forms were further separated by size exclusion chromatography, but could not be isolated to purity. All AFPs in the hemolymph of this species appears to have isoelectric points above 8.00. The dominant form, RiAFP
H4, was purified by the ion exchange step. Its amino acid composition reveals a lower level of cysteine and a higher level of threonine, arginine, alanine and glycine than seen in other insect AFPs. Its trypsin fingerprint does not match that of any known protein. It interacts with ice both in the anionic and cationic state.</description><subject>Alanine - chemistry</subject><subject>Amino Acids - chemistry</subject><subject>Amino Acids - metabolism</subject><subject>Animals</subject><subject>Antifreeze protein</subject><subject>Antifreeze Proteins - chemistry</subject><subject>Antifreeze Proteins - isolation & purification</subject><subject>Arginine - chemistry</subject><subject>Beetle</subject><subject>Cations</subject><subject>Cerambycidae</subject><subject>Chromatography, Ion Exchange</subject><subject>Coleoptera - metabolism</subject><subject>Cysteine - chemistry</subject><subject>Glycine - chemistry</subject><subject>Hemolymph</subject><subject>Hemolymph - chemistry</subject><subject>Hemolymph - metabolism</subject><subject>Insect</subject><subject>Isoelectric Focusing</subject><subject>Larva - metabolism</subject><subject>Mass Spectrometry</subject><subject>Rhagium inquisitor</subject><subject>Threonine - chemistry</subject><issn>1096-4959</issn><issn>1879-1107</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU2L1TAUhoMozof-AReSleiiNWmaNAE3w6DjwAVBdB3S5HSaS9vcSdKBub_elHvBna5ykvOcl0MehN5RUlNCxed9bfuDrRtCeE1ETUj7Al1S2amKUtK9LDVRomoVVxfoKqU9IUxSRl-jC8qVYoLJS3S8T2Ey2YcFm8VhO5pobIboj6fHMOAR5jA9z4exENkPEeAI-BBDBr8kPMQw48nEJwMbnEfAU1gexhAX3APkCfDP0Tz4dcZ-eVx98jlE_HFXf3qDXg1mSvD2fF6j39--_rr9Xu1-3N3f3uwqyyTPlVOMN6Y3DeemE9CT3vUd7x1jzpABDHUAiriWg4RGSdeq0pC23LkxRFh2jT6ccsvOjyukrGefLEyTWSCsSQvZctJI9V-Qdi1njdjA5gTaGFKKMOhD9LOJz5oSvanRe72p0ZsaTYQuasrQ-3P62s_g_o6cXRTgywmA8hlPHqJO1sNiwfkINmsX_L_y_wBcUqK_</recordid><startdate>20050901</startdate><enddate>20050901</enddate><creator>Kristiansen, E.</creator><creator>Ramløv, H.</creator><creator>Hagen, L.</creator><creator>Pedersen, S.A.</creator><creator>Andersen, R.A.</creator><creator>Zachariassen, K.E.</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>7SS</scope><scope>7X8</scope></search><sort><creationdate>20050901</creationdate><title>Isolation and characterization of hemolymph antifreeze proteins from larvae of the longhorn beetle Rhagium inquisitor (L.)</title><author>Kristiansen, E. ; Ramløv, H. ; Hagen, L. ; Pedersen, S.A. ; Andersen, R.A. ; Zachariassen, K.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c385t-d9352aba255a76eb0bdb75bd33da0fea1dee90d45e8e298d493da8c45e5aa06c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Alanine - chemistry</topic><topic>Amino Acids - chemistry</topic><topic>Amino Acids - metabolism</topic><topic>Animals</topic><topic>Antifreeze protein</topic><topic>Antifreeze Proteins - chemistry</topic><topic>Antifreeze Proteins - isolation & purification</topic><topic>Arginine - chemistry</topic><topic>Beetle</topic><topic>Cations</topic><topic>Cerambycidae</topic><topic>Chromatography, Ion Exchange</topic><topic>Coleoptera - metabolism</topic><topic>Cysteine - chemistry</topic><topic>Glycine - chemistry</topic><topic>Hemolymph</topic><topic>Hemolymph - chemistry</topic><topic>Hemolymph - metabolism</topic><topic>Insect</topic><topic>Isoelectric Focusing</topic><topic>Larva - metabolism</topic><topic>Mass Spectrometry</topic><topic>Rhagium inquisitor</topic><topic>Threonine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kristiansen, E.</creatorcontrib><creatorcontrib>Ramløv, H.</creatorcontrib><creatorcontrib>Hagen, L.</creatorcontrib><creatorcontrib>Pedersen, S.A.</creatorcontrib><creatorcontrib>Andersen, R.A.</creatorcontrib><creatorcontrib>Zachariassen, K.E.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><jtitle>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kristiansen, E.</au><au>Ramløv, H.</au><au>Hagen, L.</au><au>Pedersen, S.A.</au><au>Andersen, R.A.</au><au>Zachariassen, K.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and characterization of hemolymph antifreeze proteins from larvae of the longhorn beetle Rhagium inquisitor (L.)</atitle><jtitle>Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology</jtitle><addtitle>Comp Biochem Physiol B Biochem Mol Biol</addtitle><date>2005-09-01</date><risdate>2005</risdate><volume>142</volume><issue>1</issue><spage>90</spage><epage>97</epage><pages>90-97</pages><issn>1096-4959</issn><eissn>1879-1107</eissn><abstract>We describe a simple and effective procedure to isolate antifreeze proteins (AFPs) from the hemolymph of larvae of the longhorn beetle
Rhagium inquisitor, and present some characteristics of their structures. Several AFPs were isolated from the hemolymph of this species by heat and acid extraction followed by cation exchange. The hemolymph contains at least six AFPs ranging in size from 12.5 to 12.8 kDa. Of these, three were separated to purity by the ion exchange step, as indicated by mass spectrometry. The remaining three forms were further separated by size exclusion chromatography, but could not be isolated to purity. All AFPs in the hemolymph of this species appears to have isoelectric points above 8.00. The dominant form, RiAFP
H4, was purified by the ion exchange step. Its amino acid composition reveals a lower level of cysteine and a higher level of threonine, arginine, alanine and glycine than seen in other insect AFPs. Its trypsin fingerprint does not match that of any known protein. It interacts with ice both in the anionic and cationic state.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>15993638</pmid><doi>10.1016/j.cbpc.2005.06.004</doi><tpages>8</tpages></addata></record> |
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| subjects | Alanine - chemistry Amino Acids - chemistry Amino Acids - metabolism Animals Antifreeze protein Antifreeze Proteins - chemistry Antifreeze Proteins - isolation & purification Arginine - chemistry Beetle Cations Cerambycidae Chromatography, Ion Exchange Coleoptera - metabolism Cysteine - chemistry Glycine - chemistry Hemolymph Hemolymph - chemistry Hemolymph - metabolism Insect Isoelectric Focusing Larva - metabolism Mass Spectrometry Rhagium inquisitor Threonine - chemistry |
| title | Isolation and characterization of hemolymph antifreeze proteins from larvae of the longhorn beetle Rhagium inquisitor (L.) |
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