Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor.
Identifieur interne : 000022 ( Ncbi/Merge ); précédent : 000021; suivant : 000023Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor.
Auteurs : L O Narhi [États-Unis] ; J S Philo ; B. Sun ; B S Chang ; T. ArakawaSource :
- Pharmaceutical research [ 0724-8741 ] ; 1999.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Recombinant Proteins, Thrombopoietin.
- chemical , pharmacology : Sucrose, Urea.
- chemical : Buffers.
- Circular Dichroism, Hot Temperature, Humans, Osmolar Concentration, Protein Conformation, Protein Denaturation, Protein Folding, Surface Tension.
Abstract
The present study was performed to examine the effect of solution conditions on the reversibility of the thermal denaturation of megakaryocyte growth and development factor (rHuMGDF).
DOI: 10.1023/a:1018893115557
PubMed: 10397597
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor.</title><author><name sortKey="Narhi, L O" sort="Narhi, L O" uniqKey="Narhi L" first="L O" last="Narhi">L O Narhi</name><affiliation wicri:level="1"><nlm:affiliation>Amgen Inc., Amgen Center, Thousand Oaks, California 91320, USA. lnarhi@amgen.com</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Amgen Inc., Amgen Center, Thousand Oaks, California 91320</wicri:regionArea><wicri:noRegion>California 91320</wicri:noRegion></affiliation></author><author><name sortKey="Philo, J S" sort="Philo, J S" uniqKey="Philo J" first="J S" last="Philo">J S Philo</name></author><author><name sortKey="Sun, B" sort="Sun, B" uniqKey="Sun B" first="B" last="Sun">B. Sun</name></author><author><name sortKey="Chang, B S" sort="Chang, B S" uniqKey="Chang B" first="B S" last="Chang">B S Chang</name></author><author><name sortKey="Arakawa, T" sort="Arakawa, T" uniqKey="Arakawa T" first="T" last="Arakawa">T. Arakawa</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10397597</idno><idno type="pmid">10397597</idno><idno type="doi">10.1023/a:1018893115557</idno><idno type="wicri:Area/PubMed/Corpus">002627</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002627</idno><idno type="wicri:Area/PubMed/Curation">002627</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002627</idno><idno type="wicri:Area/PubMed/Checkpoint">002472</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002472</idno><idno type="wicri:Area/Ncbi/Merge">000022</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor.</title><author><name sortKey="Narhi, L O" sort="Narhi, L O" uniqKey="Narhi L" first="L O" last="Narhi">L O Narhi</name><affiliation wicri:level="1"><nlm:affiliation>Amgen Inc., Amgen Center, Thousand Oaks, California 91320, USA. lnarhi@amgen.com</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Amgen Inc., Amgen Center, Thousand Oaks, California 91320</wicri:regionArea><wicri:noRegion>California 91320</wicri:noRegion></affiliation></author><author><name sortKey="Philo, J S" sort="Philo, J S" uniqKey="Philo J" first="J S" last="Philo">J S Philo</name></author><author><name sortKey="Sun, B" sort="Sun, B" uniqKey="Sun B" first="B" last="Sun">B. Sun</name></author><author><name sortKey="Chang, B S" sort="Chang, B S" uniqKey="Chang B" first="B S" last="Chang">B S Chang</name></author><author><name sortKey="Arakawa, T" sort="Arakawa, T" uniqKey="Arakawa T" first="T" last="Arakawa">T. Arakawa</name></author></analytic><series><title level="j">Pharmaceutical research</title><idno type="ISSN">0724-8741</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Buffers</term><term>Circular Dichroism</term><term>Hot Temperature</term><term>Humans</term><term>Osmolar Concentration</term><term>Protein Conformation</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Recombinant Proteins (chemistry)</term><term>Sucrose (pharmacology)</term><term>Surface Tension</term><term>Thrombopoietin (chemistry)</term><term>Urea (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Concentration osmolaire</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Dénaturation des protéines</term><term>Humains</term><term>Pliage des protéines</term><term>Protéines recombinantes ()</term><term>Saccharose (pharmacologie)</term><term>Substances tampon</term><term>Température élevée</term><term>Tension superficielle</term><term>Thrombopoïétine ()</term><term>Urée (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term><term>Thrombopoietin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sucrose</term><term>Urea</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Buffers</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Saccharose</term><term>Urée</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term><term>Hot Temperature</term><term>Humans</term><term>Osmolar Concentration</term><term>Protein Conformation</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Surface Tension</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration osmolaire</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Dénaturation des protéines</term><term>Humains</term><term>Pliage des protéines</term><term>Protéines recombinantes</term><term>Substances tampon</term><term>Température élevée</term><term>Tension superficielle</term><term>Thrombopoïétine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The present study was performed to examine the effect of solution conditions on the reversibility of the thermal denaturation of megakaryocyte growth and development factor (rHuMGDF).</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10397597</PMID><DateCompleted><Year>1999</Year><Month>08</Month><Day>18</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0724-8741</ISSN><JournalIssue CitedMedium="Print"><Volume>16</Volume><Issue>6</Issue><PubDate><Year>1999</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Pharmaceutical research</Title><ISOAbbreviation>Pharm. Res.</ISOAbbreviation></Journal><ArticleTitle>Reversibility of heat-induced denaturation of the recombinant human megakaryocyte growth and development factor.</ArticleTitle><Pagination><MedlinePgn>799-807</MedlinePgn></Pagination><Abstract><AbstractText Label="PURPOSE" NlmCategory="OBJECTIVE">The present study was performed to examine the effect of solution conditions on the reversibility of the thermal denaturation of megakaryocyte growth and development factor (rHuMGDF).</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">Changes in the far UV CD spectra of rHuMGDF with temperature were used to monitor the thermal denaturation of the protein, and the recovery of folded protein following a return to room temperature. The effect of protein concentration, scan rate, and buffer composition on thermal denaturation and on the reversibility were determined. Surface tension measurements were used to determine the effect of this unfolding reaction on the surface adsorption of the protein. Sedimentation velocity was used to assess recovery of native monomer and the size of soluble aggregates. In addition, monomeric protein remaining in solution after incubation at 37 degrees C for 2 weeks in either 10 mM imidazole of 10 mM phosphate was determined.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">In phosphate buffer the rHuMGDF irreversibly precipitates upon unfolding under all the conditions examined. In imidazole the unfolding is at least partially reversible, with no visible precipitate seen; the degree of reversibility increased by lowering both protein and salt concentrations, and the amount of time spent at elevated temperature. In order to compare thermal unfolding occuring with different degrees of reversibility, the melting temperature was defined as the temperature at which melting begins. The melting temperature itself is relatively independent of the buffer composition, or experimental conditions. At low protein concentrations the protein stabilizer sucrose had a marginal effect on the thermal transition of rHuMGDF, while at protein concentrations of about 2 mg/ml the inclusion of sucrose increased the apparent melting temperature by about 4 degrees C, to that seen at low protein concentrations, but had little effect on the reversibility of denaturation. Inclusion of 1 or 2 M urea did not affect the reaction. Surface tension measurements of rHuMGDF solutions showed little difference before and after melting, and in the presence or absence of sucrose. When unfolding is irreversible, the MGDF appears to form soluble aggregates of tetramers to 14-mers, while under reversible conditions native monomer is recovered. More monomeric MGDF remained in solution following storage for 2 weeks at 37 degrees C in imidazole than in phosphate, in both the presence and absence of sucrose.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">These results can be explained by assuming that thermal denaturation proceeds as a two-step reaction, the first step being the equilibrium between folded and unfolded states, while the second step is a slow irreversible aggregation. The different buffer systems affect the rate of the aggregation step, but not the intrinsic thermal stability nor the rate of the unfolding step.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Narhi</LastName><ForeName>L O</ForeName><Initials>LO</Initials><AffiliationInfo><Affiliation>Amgen Inc., Amgen Center, Thousand Oaks, California 91320, USA. lnarhi@amgen.com</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Philo</LastName><ForeName>J S</ForeName><Initials>JS</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>B S</ForeName><Initials>BS</Initials></Author><Author ValidYN="Y"><LastName>Arakawa</LastName><ForeName>T</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Pharm Res</MedlineTA><NlmUniqueID>8406521</NlmUniqueID><ISSNLinking>0724-8741</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002021">Buffers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>57-50-1</RegistryNumber><NameOfSubstance UI="D013395">Sucrose</NameOfSubstance></Chemical><Chemical><RegistryNumber>8W8T17847W</RegistryNumber><NameOfSubstance UI="D014508">Urea</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-42-0</RegistryNumber><NameOfSubstance UI="D013926">Thrombopoietin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002021" MajorTopicYN="N">Buffers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009994" MajorTopicYN="N">Osmolar Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" 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PubStatus="entrez"><Year>1999</Year><Month>7</Month><Day>9</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10397597</ArticleId><ArticleId IdType="doi">10.1023/a:1018893115557</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biol Chem. 1981 Jul 25;256(14):7193-201</Citation><ArticleIdList><ArticleId IdType="pubmed">7251592</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1982 Dec 7;21(25):6536-44</Citation><ArticleIdList><ArticleId IdType="pubmed">7150574</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1979 Nov 13;18(23):5191-6</Citation><ArticleIdList><ArticleId IdType="pubmed">497177</ArticleId></ArticleIdList></Reference><Reference><Citation>Int J Biol Macromol. 1991 Dec;13(6):322-8</Citation><ArticleIdList><ArticleId IdType="pubmed">1772822</ArticleId></ArticleIdList></Reference><Reference><Citation>J Pharm Sci. 1996 Apr;85(4):419-26</Citation><ArticleIdList><ArticleId IdType="pubmed">8901081</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1994 Jun 16;369(6481):533-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8202154</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1994 Jul 1;77(7):1117-24</Citation><ArticleIdList><ArticleId IdType="pubmed">8020099</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1994 Dec 20;33(50):15178-89</Citation><ArticleIdList><ArticleId IdType="pubmed">7999778</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Hematol. 1995 May;2(3):172-6</Citation><ArticleIdList><ArticleId IdType="pubmed">9371991</ArticleId></ArticleIdList></Reference><Reference><Citation>N Engl J Med. 1997 Feb 6;336(6):404-9</Citation><ArticleIdList><ArticleId IdType="pubmed">9010146</ArticleId></ArticleIdList></Reference><Reference><Citation>J Pharm Sci. 1994 Dec;83(12 ):1657-61</Citation><ArticleIdList><ArticleId IdType="pubmed">7891291</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Sci. 1998 Jul;7(7):1538-44</Citation><ArticleIdList><ArticleId IdType="pubmed">9684886</ArticleId></ArticleIdList></Reference><Reference><Citation>Blood. 1997 May 1;89(9):3118-28</Citation><ArticleIdList><ArticleId IdType="pubmed">9129014</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1994 Jun 16;369(6481):565-8</Citation><ArticleIdList><ArticleId IdType="pubmed">8202158</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1993 Nov 20;234(2):463-82</Citation><ArticleIdList><ArticleId IdType="pubmed">8230226</ArticleId></ArticleIdList></Reference><Reference><Citation>Pharm Res. 1996 May;13(5):756-61</Citation><ArticleIdList><ArticleId IdType="pubmed">8860433</ArticleId></ArticleIdList></Reference><Reference><Citation>J Protein Chem. 1995 Nov;14(8):709-19</Citation><ArticleIdList><ArticleId IdType="pubmed">8747432</ArticleId></ArticleIdList></Reference><Reference><Citation>Biophys J. 1997 Jan;72(1):435-44</Citation><ArticleIdList><ArticleId IdType="pubmed">8994630</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1992 Jun;203(2):295-301</Citation><ArticleIdList><ArticleId IdType="pubmed">1416025</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Biol. 1994 Sep 30;242(4):321-9</Citation><ArticleIdList><ArticleId IdType="pubmed">7932692</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1981 Sep;210(2):455-64</Citation><ArticleIdList><ArticleId IdType="pubmed">7305338</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Arakawa, T" sort="Arakawa, T" uniqKey="Arakawa T" first="T" last="Arakawa">T. Arakawa</name><name sortKey="Chang, B S" sort="Chang, B S" uniqKey="Chang B" first="B S" last="Chang">B S Chang</name><name sortKey="Philo, J S" sort="Philo, J S" uniqKey="Philo J" first="J S" last="Philo">J S Philo</name><name sortKey="Sun, B" sort="Sun, B" uniqKey="Sun B" first="B" last="Sun">B. Sun</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Narhi, L O" sort="Narhi, L O" uniqKey="Narhi L" first="L O" last="Narhi">L O Narhi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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