Self-association of rabbit muscle phosphofructokinase at pH 7.0: stoichiometry
The self-association of rabbit muscle phosphofructokinase at pH 7.0 was investigated by velocity sedimentation. The process was demonstrated to be in a rapid, dynamic equilibrium. The concentration dependence of the weight-average sedimentation coefficient was monitored within the range of 10-750 mi...
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| Veröffentlicht in: | Biochemistry (Easton) 1981-05, Vol.20 (10), p.2974-2980 |
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| creator | Hesterberg, Lyndal K Lee, James C |
| description | The self-association of rabbit muscle phosphofructokinase at pH 7.0 was investigated by velocity sedimentation. The process was demonstrated to be in a rapid, dynamic equilibrium. The concentration dependence of the weight-average sedimentation coefficient was monitored within the range of 10-750 microgram/mL. The sedimentation properties of phosphofructokinase were analyzed by theoretical simulations or an associating system in rapid equilibrium. In the absence of any ligands and at a temperature of 23 degrees C, the simplest computed model which gives the best fit between theoretical and experimental points can be described as progressive association of monomer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer with apparent equilibrium constants K4 = 5.06 X 10(5) (mL/mg)3 and K16 = 3.25 X 10(23) (mL/mg)15. However, at 5 degrees C, the equilibrium was altered and can best be described as monomer in equilibrium or formed from dimer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer. |
| doi_str_mv | 10.1021/bi00513a040 |
| format | Article |
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The process was demonstrated to be in a rapid, dynamic equilibrium. The concentration dependence of the weight-average sedimentation coefficient was monitored within the range of 10-750 microgram/mL. The sedimentation properties of phosphofructokinase were analyzed by theoretical simulations or an associating system in rapid equilibrium. In the absence of any ligands and at a temperature of 23 degrees C, the simplest computed model which gives the best fit between theoretical and experimental points can be described as progressive association of monomer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer with apparent equilibrium constants K4 = 5.06 X 10(5) (mL/mg)3 and K16 = 3.25 X 10(23) (mL/mg)15. However, at 5 degrees C, the equilibrium was altered and can best be described as monomer in equilibrium or formed from dimer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00513a040</identifier><identifier>PMID: 6454440</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Hydrogen-Ion Concentration ; Kinetics ; Macromolecular Substances ; Mathematics ; Molecular Weight ; Muscles - enzymology ; Phosphofructokinase-1 - metabolism ; Rabbits</subject><ispartof>Biochemistry (Easton), 1981-05, Vol.20 (10), p.2974-2980</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a354t-c2cce0bea767b2719e22bc0060318ada5fb0732573c3e94330ec781f77cdad363</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi00513a040$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00513a040$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6454440$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hesterberg, Lyndal K</creatorcontrib><creatorcontrib>Lee, James C</creatorcontrib><title>Self-association of rabbit muscle phosphofructokinase at pH 7.0: stoichiometry</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>The self-association of rabbit muscle phosphofructokinase at pH 7.0 was investigated by velocity sedimentation. The process was demonstrated to be in a rapid, dynamic equilibrium. The concentration dependence of the weight-average sedimentation coefficient was monitored within the range of 10-750 microgram/mL. The sedimentation properties of phosphofructokinase were analyzed by theoretical simulations or an associating system in rapid equilibrium. In the absence of any ligands and at a temperature of 23 degrees C, the simplest computed model which gives the best fit between theoretical and experimental points can be described as progressive association of monomer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer with apparent equilibrium constants K4 = 5.06 X 10(5) (mL/mg)3 and K16 = 3.25 X 10(23) (mL/mg)15. However, at 5 degrees C, the equilibrium was altered and can best be described as monomer in equilibrium or formed from dimer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer.</description><subject>Animals</subject><subject>Hydrogen-Ion Concentration</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Mathematics</subject><subject>Molecular Weight</subject><subject>Muscles - enzymology</subject><subject>Phosphofructokinase-1 - metabolism</subject><subject>Rabbits</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1LxDAQhoMouq6ePAs96UGqk69m600W1xX8QlfwFtI0ZaPtpiYp6L-30mXx4GEYhvdhZngQOsJwjoHgi8ICcEwVMNhCI8wJpCzP-TYaAUCWkjyDPbQfwns_MhBsF-1mjDPGYIQeXkxdpSoEp62K1q0SVyVeFYWNSdMFXZukXbrQV-U7Hd2HXalgEhWTdp6Ic7hMQnRWL61rTPTfB2inUnUwh-s-Rq-z68V0nt493txOr-5SRTmLqSZaGyiMEpkoiMC5IaTQ_bNA8USVilcFCEq4oJqanFEKRosJroTQpSppRsfoZNjbevfZmRBlY4M2da1WxnVBCsopzQXpwbMB1N6F4E0lW28b5b8lBvlrT_6x19PH67Vd0Zhyw6519Xk65DZE87WJlf-QmaCCy8XTi5zdv91M5osH-dzzpwOvdJDvrvOrXsq_l38AHziFfg</recordid><startdate>19810512</startdate><enddate>19810512</enddate><creator>Hesterberg, Lyndal K</creator><creator>Lee, James C</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>19810512</creationdate><title>Self-association of rabbit muscle phosphofructokinase at pH 7.0: stoichiometry</title><author>Hesterberg, Lyndal K ; Lee, James C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a354t-c2cce0bea767b2719e22bc0060318ada5fb0732573c3e94330ec781f77cdad363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>Animals</topic><topic>Hydrogen-Ion Concentration</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Mathematics</topic><topic>Molecular Weight</topic><topic>Muscles - enzymology</topic><topic>Phosphofructokinase-1 - metabolism</topic><topic>Rabbits</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hesterberg, Lyndal K</creatorcontrib><creatorcontrib>Lee, James C</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hesterberg, Lyndal K</au><au>Lee, James C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Self-association of rabbit muscle phosphofructokinase at pH 7.0: stoichiometry</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1981-05-12</date><risdate>1981</risdate><volume>20</volume><issue>10</issue><spage>2974</spage><epage>2980</epage><pages>2974-2980</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The self-association of rabbit muscle phosphofructokinase at pH 7.0 was investigated by velocity sedimentation. The process was demonstrated to be in a rapid, dynamic equilibrium. The concentration dependence of the weight-average sedimentation coefficient was monitored within the range of 10-750 microgram/mL. The sedimentation properties of phosphofructokinase were analyzed by theoretical simulations or an associating system in rapid equilibrium. In the absence of any ligands and at a temperature of 23 degrees C, the simplest computed model which gives the best fit between theoretical and experimental points can be described as progressive association of monomer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer with apparent equilibrium constants K4 = 5.06 X 10(5) (mL/mg)3 and K16 = 3.25 X 10(23) (mL/mg)15. However, at 5 degrees C, the equilibrium was altered and can best be described as monomer in equilibrium or formed from dimer in equilibrium or formed from tetramer in equilibrium or formed from 16-mer.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>6454440</pmid><doi>10.1021/bi00513a040</doi><tpages>7</tpages></addata></record> |
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| issn | 0006-2960 1520-4995 |
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| source | MEDLINE; American Chemical Society (ACS) Journals |
| subjects | Animals Hydrogen-Ion Concentration Kinetics Macromolecular Substances Mathematics Molecular Weight Muscles - enzymology Phosphofructokinase-1 - metabolism Rabbits |
| title | Self-association of rabbit muscle phosphofructokinase at pH 7.0: stoichiometry |
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