Temperature and pH dependence of immunoglobulin G conformation
Previous indirect observations have indicated that IgG may change its conformation at low or high pH and at a temperature of about 35 °C. By means of small angle neutron scattering a change in the value of the gyration radius of two different native IgG's was observed above 44 °C. No similar ch...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1991-12, Vol.291 (2), p.277-283 |
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| container_title | Archives of biochemistry and biophysics |
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| creator | Calmettes, P. Cser, L. Rajnavölgyi, É. |
| description | Previous indirect observations have indicated that IgG may change its conformation at low or high pH and at a temperature of about 35 °C. By means of small angle neutron scattering a change in the value of the gyration radius of two different native IgG's was observed above 44 °C. No similar change was detected when the sample was previously dissolved in an acidic buffer. The acidic pretreatment caused a significant decrease in the gyration radius (
R
g
) value measured at 20 °C which was partially recovered by increasing the temperature. These observations led to the assumption that the main conformational change observed appears either in the hinge region of the molecule or in the interdomain areas separating the constant and the variable domains of the Fab parts. |
| doi_str_mv | 10.1016/0003-9861(91)90135-6 |
| format | Article |
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R
g
) value measured at 20 °C which was partially recovered by increasing the temperature. These observations led to the assumption that the main conformational change observed appears either in the hinge region of the molecule or in the interdomain areas separating the constant and the variable domains of the Fab parts.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(91)90135-6</identifier><identifier>PMID: 1952941</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Animals ; Antibodies, immunoglobulins ; Biological and medical sciences ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; Humans ; Hydrogen-Ion Concentration ; Immunoglobulin G - chemistry ; Immunoglobulin Isotypes - chemistry ; Molecular immunology ; Phenylhydrazines - chemistry ; Phenylhydrazines - immunology ; Protein Conformation ; Structure ; Swine ; Temperature</subject><ispartof>Archives of biochemistry and biophysics, 1991-12, Vol.291 (2), p.277-283</ispartof><rights>1991</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c417t-81c46335f94ff170e585bdd4b62e5fac30a4983d309cd949ea187d1398ec7d783</citedby><cites>FETCH-LOGICAL-c417t-81c46335f94ff170e585bdd4b62e5fac30a4983d309cd949ea187d1398ec7d783</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0003986191901356$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5060346$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1952941$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Calmettes, P.</creatorcontrib><creatorcontrib>Cser, L.</creatorcontrib><creatorcontrib>Rajnavölgyi, É.</creatorcontrib><title>Temperature and pH dependence of immunoglobulin G conformation</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>Previous indirect observations have indicated that IgG may change its conformation at low or high pH and at a temperature of about 35 °C. By means of small angle neutron scattering a change in the value of the gyration radius of two different native IgG's was observed above 44 °C. No similar change was detected when the sample was previously dissolved in an acidic buffer. The acidic pretreatment caused a significant decrease in the gyration radius (
R
g
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R
g
) value measured at 20 °C which was partially recovered by increasing the temperature. These observations led to the assumption that the main conformational change observed appears either in the hinge region of the molecule or in the interdomain areas separating the constant and the variable domains of the Fab parts.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1952941</pmid><doi>10.1016/0003-9861(91)90135-6</doi><tpages>7</tpages></addata></record> |
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| ispartof | Archives of biochemistry and biophysics, 1991-12, Vol.291 (2), p.277-283 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Antibodies, immunoglobulins Biological and medical sciences Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Hydrogen-Ion Concentration Immunoglobulin G - chemistry Immunoglobulin Isotypes - chemistry Molecular immunology Phenylhydrazines - chemistry Phenylhydrazines - immunology Protein Conformation Structure Swine Temperature |
| title | Temperature and pH dependence of immunoglobulin G conformation |
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