Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C
1. 1. The results of chemically crosslinking yeast cytochrome c peroxidase with both horse and yeast iso-1 ferricytochromes c have been studied by a combination of gel electrophoresis and proton NMR spectroscopy. 2. 2. The complexes were formed at a variety of potassium phosphate concentrations rang...
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| Veröffentlicht in: | International journal of biochemistry 1993, Vol.25 (9), p.1335-1342 |
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| container_title | International journal of biochemistry |
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| creator | Moench, S.J. Erman, J.E. Satterlee, J.D. |
| description | 1.
1. The results of chemically crosslinking yeast cytochrome
c peroxidase with both horse and yeast iso-1 ferricytochromes
c have been studied by a combination of gel electrophoresis and proton NMR spectroscopy.
2.
2. The complexes were formed at a variety of potassium phosphate concentrations ranging from 10 to 300 mM using the water soluble crosslinking agent, EDC (l-ethyl-3-[3-(dimethylamino)propyl]-carbodiimide).
3.
3. The primary crosslinking product in both cases is the 1:1 covalent complex, but, for each pair of partner proteins the yield of the 1:1 crosslinked complex varies with the salt concentration.
4.
4. Furthermore, at low salt concentrations the yield of the 1:1 covalent complex involving horse cytochrome
c is much larger than the yield of the 1:1 covalent complex formed with yeast iso-1 cytochrome
c, whereas at high salt concentrations the situation is reversed.
5.
5. Proton NMR spectroscopy, in combination with gel electrophoresis, provides evidence for the formation of different types of 1:1 complexes for the peroxidase/yeast cytochrome
c pair and has been used to study the effect of changes in the solution ionic strength upon both the peroxidases/horse cytochrome
c and the peroxidase/yeast cytochrome
c complexes.
6.
6. This work indicates that electrostatic interactions between proteins play a dominant role in formation of complexes between cytochrome
c peroxidase and horse ferricytochrome
c, whereas the hydrophobic effect plays a comparatively larger role in stabilizing complexes between cytochrome
c peroxidase and yeast iso-1 ferricytochrome
c. |
| doi_str_mv | 10.1016/0020-711X(93)90087-U |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_75983060</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0020711X9390087U</els_id><sourcerecordid>75983060</sourcerecordid><originalsourceid>FETCH-LOGICAL-c356t-1a779c8e4decde71c5465befe8234fa4eb93fae2371c6d9d60560e9d3f23946c3</originalsourceid><addsrcrecordid>eNqFkc1u1DAQgH0AlVJ4AxA-IASHgH8Sx75UQit-KlXqYVmJm-W1x6whiYOdLd2n4JVxutFyg9NYM9_MWPMh9IySt5RQ8Y4QRqqW0q-vFX-jCJFttXmAzk_pR-hxzt8JoUrW9AydScZqLsk5-r0ewQbIVZ6jDxa74D0kGCxkHAZs463pYJi6A7Yp5tyF4Qe4ku7HDu4KEz0-gMkTtocp2l2KPeAVHiHFu-BMBvwrTDu8i6k8zeAW-Gp9U1FcFqXwty_j1RP00Jsuw9MlXqDNxw9fVp-r65tPV6v315XljZgqatpWWQm1A-ugpbapRbMFD5Lx2psatop7A4yXknDKCdIIAspxz7iqheUX6NVx7pjizz3kSfchW-g6M0DcZ902SnIiyH9BKoQUjLEC1kfw_kwJvB5T6E06aEr0LEnPNvRsQyuu7yXpTWl7vszfb3twp6bFUKm_XOomW9P5ZAYb8gnjUgrVzNiLI-ZN1OZbKshmzQjlhNaSMEULcXkkoJz1NkDSuYgvml1IYCftYvj3T_8Adqe8bQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>16686222</pqid></control><display><type>article</type><title>Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><creator>Moench, S.J. ; Erman, J.E. ; Satterlee, J.D.</creator><creatorcontrib>Moench, S.J. ; Erman, J.E. ; Satterlee, J.D.</creatorcontrib><description>1.
1. The results of chemically crosslinking yeast cytochrome
c peroxidase with both horse and yeast iso-1 ferricytochromes
c have been studied by a combination of gel electrophoresis and proton NMR spectroscopy.
2.
2. The complexes were formed at a variety of potassium phosphate concentrations ranging from 10 to 300 mM using the water soluble crosslinking agent, EDC (l-ethyl-3-[3-(dimethylamino)propyl]-carbodiimide).
3.
3. The primary crosslinking product in both cases is the 1:1 covalent complex, but, for each pair of partner proteins the yield of the 1:1 crosslinked complex varies with the salt concentration.
4.
4. Furthermore, at low salt concentrations the yield of the 1:1 covalent complex involving horse cytochrome
c is much larger than the yield of the 1:1 covalent complex formed with yeast iso-1 cytochrome
c, whereas at high salt concentrations the situation is reversed.
5.
5. Proton NMR spectroscopy, in combination with gel electrophoresis, provides evidence for the formation of different types of 1:1 complexes for the peroxidase/yeast cytochrome
c pair and has been used to study the effect of changes in the solution ionic strength upon both the peroxidases/horse cytochrome
c and the peroxidase/yeast cytochrome
c complexes.
6.
6. This work indicates that electrostatic interactions between proteins play a dominant role in formation of complexes between cytochrome
c peroxidase and horse ferricytochrome
c, whereas the hydrophobic effect plays a comparatively larger role in stabilizing complexes between cytochrome
c peroxidase and yeast iso-1 ferricytochrome
c.</description><identifier>ISSN: 0020-711X</identifier><identifier>DOI: 10.1016/0020-711X(93)90087-U</identifier><identifier>PMID: 8224380</identifier><language>eng</language><publisher>Oxford: Elsevier B.V</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; binding ; Biological and medical sciences ; Cross-Linking Reagents ; cytochrome c ; Cytochrome c Group - chemistry ; Cytochrome-c Peroxidase - chemistry ; Electrophoresis, Polyacrylamide Gel ; Enzymes and enzyme inhibitors ; Ethyldimethylaminopropyl Carbodiimide ; Fundamental and applied biological sciences. Psychology ; horses ; Horses - metabolism ; interactions ; Isoenzymes - chemistry ; Magnetic Resonance Spectroscopy ; Osmolar Concentration ; Oxidoreductases ; peroxidases ; Phenylalanine - chemistry ; Protons ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Solutions ; species differences ; Species Specificity ; yeasts</subject><ispartof>International journal of biochemistry, 1993, Vol.25 (9), p.1335-1342</ispartof><rights>1993</rights><rights>1994 INIST-CNRS</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-1a779c8e4decde71c5465befe8234fa4eb93fae2371c6d9d60560e9d3f23946c3</citedby><cites>FETCH-LOGICAL-c356t-1a779c8e4decde71c5465befe8234fa4eb93fae2371c6d9d60560e9d3f23946c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3886950$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8224380$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moench, S.J.</creatorcontrib><creatorcontrib>Erman, J.E.</creatorcontrib><creatorcontrib>Satterlee, J.D.</creatorcontrib><title>Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C</title><title>International journal of biochemistry</title><addtitle>Int J Biochem</addtitle><description>1.
1. The results of chemically crosslinking yeast cytochrome
c peroxidase with both horse and yeast iso-1 ferricytochromes
c have been studied by a combination of gel electrophoresis and proton NMR spectroscopy.
2.
2. The complexes were formed at a variety of potassium phosphate concentrations ranging from 10 to 300 mM using the water soluble crosslinking agent, EDC (l-ethyl-3-[3-(dimethylamino)propyl]-carbodiimide).
3.
3. The primary crosslinking product in both cases is the 1:1 covalent complex, but, for each pair of partner proteins the yield of the 1:1 crosslinked complex varies with the salt concentration.
4.
4. Furthermore, at low salt concentrations the yield of the 1:1 covalent complex involving horse cytochrome
c is much larger than the yield of the 1:1 covalent complex formed with yeast iso-1 cytochrome
c, whereas at high salt concentrations the situation is reversed.
5.
5. Proton NMR spectroscopy, in combination with gel electrophoresis, provides evidence for the formation of different types of 1:1 complexes for the peroxidase/yeast cytochrome
c pair and has been used to study the effect of changes in the solution ionic strength upon both the peroxidases/horse cytochrome
c and the peroxidase/yeast cytochrome
c complexes.
6.
6. This work indicates that electrostatic interactions between proteins play a dominant role in formation of complexes between cytochrome
c peroxidase and horse ferricytochrome
c, whereas the hydrophobic effect plays a comparatively larger role in stabilizing complexes between cytochrome
c peroxidase and yeast iso-1 ferricytochrome
c.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>binding</subject><subject>Biological and medical sciences</subject><subject>Cross-Linking Reagents</subject><subject>cytochrome c</subject><subject>Cytochrome c Group - chemistry</subject><subject>Cytochrome-c Peroxidase - chemistry</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Ethyldimethylaminopropyl Carbodiimide</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>horses</subject><subject>Horses - metabolism</subject><subject>interactions</subject><subject>Isoenzymes - chemistry</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Osmolar Concentration</subject><subject>Oxidoreductases</subject><subject>peroxidases</subject><subject>Phenylalanine - chemistry</subject><subject>Protons</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Solutions</subject><subject>species differences</subject><subject>Species Specificity</subject><subject>yeasts</subject><issn>0020-711X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAQgH0AlVJ4AxA-IASHgH8Sx75UQit-KlXqYVmJm-W1x6whiYOdLd2n4JVxutFyg9NYM9_MWPMh9IySt5RQ8Y4QRqqW0q-vFX-jCJFttXmAzk_pR-hxzt8JoUrW9AydScZqLsk5-r0ewQbIVZ6jDxa74D0kGCxkHAZs463pYJi6A7Yp5tyF4Qe4ku7HDu4KEz0-gMkTtocp2l2KPeAVHiHFu-BMBvwrTDu8i6k8zeAW-Gp9U1FcFqXwty_j1RP00Jsuw9MlXqDNxw9fVp-r65tPV6v315XljZgqatpWWQm1A-ugpbapRbMFD5Lx2psatop7A4yXknDKCdIIAspxz7iqheUX6NVx7pjizz3kSfchW-g6M0DcZ902SnIiyH9BKoQUjLEC1kfw_kwJvB5T6E06aEr0LEnPNvRsQyuu7yXpTWl7vszfb3twp6bFUKm_XOomW9P5ZAYb8gnjUgrVzNiLI-ZN1OZbKshmzQjlhNaSMEULcXkkoJz1NkDSuYgvml1IYCftYvj3T_8Adqe8bQ</recordid><startdate>1993</startdate><enddate>1993</enddate><creator>Moench, S.J.</creator><creator>Erman, J.E.</creator><creator>Satterlee, J.D.</creator><general>Elsevier B.V</general><general>Pergamon</general><scope>FBQ</scope><scope>IQODW</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>1993</creationdate><title>Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C</title><author>Moench, S.J. ; Erman, J.E. ; Satterlee, J.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-1a779c8e4decde71c5465befe8234fa4eb93fae2371c6d9d60560e9d3f23946c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>binding</topic><topic>Biological and medical sciences</topic><topic>Cross-Linking Reagents</topic><topic>cytochrome c</topic><topic>Cytochrome c Group - chemistry</topic><topic>Cytochrome-c Peroxidase - chemistry</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Ethyldimethylaminopropyl Carbodiimide</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>horses</topic><topic>Horses - metabolism</topic><topic>interactions</topic><topic>Isoenzymes - chemistry</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Osmolar Concentration</topic><topic>Oxidoreductases</topic><topic>peroxidases</topic><topic>Phenylalanine - chemistry</topic><topic>Protons</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Solutions</topic><topic>species differences</topic><topic>Species Specificity</topic><topic>yeasts</topic><toplevel>online_resources</toplevel><creatorcontrib>Moench, S.J.</creatorcontrib><creatorcontrib>Erman, J.E.</creatorcontrib><creatorcontrib>Satterlee, J.D.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moench, S.J.</au><au>Erman, J.E.</au><au>Satterlee, J.D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C</atitle><jtitle>International journal of biochemistry</jtitle><addtitle>Int J Biochem</addtitle><date>1993</date><risdate>1993</risdate><volume>25</volume><issue>9</issue><spage>1335</spage><epage>1342</epage><pages>1335-1342</pages><issn>0020-711X</issn><abstract>1.
1. The results of chemically crosslinking yeast cytochrome
c peroxidase with both horse and yeast iso-1 ferricytochromes
c have been studied by a combination of gel electrophoresis and proton NMR spectroscopy.
2.
2. The complexes were formed at a variety of potassium phosphate concentrations ranging from 10 to 300 mM using the water soluble crosslinking agent, EDC (l-ethyl-3-[3-(dimethylamino)propyl]-carbodiimide).
3.
3. The primary crosslinking product in both cases is the 1:1 covalent complex, but, for each pair of partner proteins the yield of the 1:1 crosslinked complex varies with the salt concentration.
4.
4. Furthermore, at low salt concentrations the yield of the 1:1 covalent complex involving horse cytochrome
c is much larger than the yield of the 1:1 covalent complex formed with yeast iso-1 cytochrome
c, whereas at high salt concentrations the situation is reversed.
5.
5. Proton NMR spectroscopy, in combination with gel electrophoresis, provides evidence for the formation of different types of 1:1 complexes for the peroxidase/yeast cytochrome
c pair and has been used to study the effect of changes in the solution ionic strength upon both the peroxidases/horse cytochrome
c and the peroxidase/yeast cytochrome
c complexes.
6.
6. This work indicates that electrostatic interactions between proteins play a dominant role in formation of complexes between cytochrome
c peroxidase and horse ferricytochrome
c, whereas the hydrophobic effect plays a comparatively larger role in stabilizing complexes between cytochrome
c peroxidase and yeast iso-1 ferricytochrome
c.</abstract><cop>Oxford</cop><pub>Elsevier B.V</pub><pmid>8224380</pmid><doi>10.1016/0020-711X(93)90087-U</doi><tpages>8</tpages></addata></record> |
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| ispartof | International journal of biochemistry, 1993, Vol.25 (9), p.1335-1342 |
| issn | 0020-711X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_75983060 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Animals binding Biological and medical sciences Cross-Linking Reagents cytochrome c Cytochrome c Group - chemistry Cytochrome-c Peroxidase - chemistry Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Ethyldimethylaminopropyl Carbodiimide Fundamental and applied biological sciences. Psychology horses Horses - metabolism interactions Isoenzymes - chemistry Magnetic Resonance Spectroscopy Osmolar Concentration Oxidoreductases peroxidases Phenylalanine - chemistry Protons Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Solutions species differences Species Specificity yeasts |
| title | Species-specific differences in covalently crosslinked complexes of yeast cytochrome C peroxidase with horse and yeast ISO-1 ferricytochromes C |
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