The Subunit Structure of Lactate Dehydrogenase from Streptococcus cremoris US3
1 Lactate dehydrogenase from Streptococcus cremoris US3, which has a molecular weight in solution of 140000, was found by dodecylsulphate‐gel electrophoresis to have a minimum molecular weight of 37000. It is, therefore, a tetramer. 2 Approximately 40 tryptic peptides were obtained by fingerprinting...
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| Veröffentlicht in: | European journal of biochemistry 1972-10, Vol.30 (2), p.348-353 |
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| container_end_page | 353 |
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| container_start_page | 348 |
| container_title | European journal of biochemistry |
| container_volume | 30 |
| creator | Dynon, Maria K. Jago, G. Richard Davidson, Barrie E. Gething, Mary Jane H. Davidson, Barrie E. |
| description | 1
Lactate dehydrogenase from Streptococcus cremoris US3, which has a molecular weight in solution of 140000, was found by dodecylsulphate‐gel electrophoresis to have a minimum molecular weight of 37000. It is, therefore, a tetramer.
2
Approximately 40 tryptic peptides were obtained by fingerprinting and in conjunction with the amino acid composition this indicates that the subunits are similar and probably identical.
3
There is one thiol group per subunit.
4
p‐Chloromercuribenzoate inhibits the enzyme. |
| doi_str_mv | 10.1111/j.1432-1033.1972.tb02104.x |
| format | Article |
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Lactate dehydrogenase from Streptococcus cremoris US3, which has a molecular weight in solution of 140000, was found by dodecylsulphate‐gel electrophoresis to have a minimum molecular weight of 37000. It is, therefore, a tetramer.
2
Approximately 40 tryptic peptides were obtained by fingerprinting and in conjunction with the amino acid composition this indicates that the subunits are similar and probably identical.
3
There is one thiol group per subunit.
4
p‐Chloromercuribenzoate inhibits the enzyme.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1972.tb02104.x</identifier><identifier>PMID: 4123271</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acids - analysis ; Benzoates ; Chloromercuribenzoates ; Chromatography, DEAE-Cellulose ; Chromatography, Gel ; Electrophoresis, Polyacrylamide Gel ; Fructosephosphates ; Indicators and Reagents ; L-Lactate Dehydrogenase - analysis ; L-Lactate Dehydrogenase - antagonists & inhibitors ; L-Lactate Dehydrogenase - isolation & purification ; Macromolecular Substances ; Molecular Weight ; NAD ; Nitro Compounds ; Peptides - analysis ; Protein Denaturation - drug effects ; Sodium Dodecyl Sulfate ; Spectrophotometry, Ultraviolet ; Staining and Labeling ; Streptococcus - enzymology ; Trypsin</subject><ispartof>European journal of biochemistry, 1972-10, Vol.30 (2), p.348-353</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4228-c70aa7dc80d90e692331001e2d0aab42aea39de4daeada6190a5a84d537cbf6e3</citedby><cites>FETCH-LOGICAL-c4228-c70aa7dc80d90e692331001e2d0aab42aea39de4daeada6190a5a84d537cbf6e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4123271$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dynon, Maria K.</creatorcontrib><creatorcontrib>Jago, G. Richard</creatorcontrib><creatorcontrib>Davidson, Barrie E.</creatorcontrib><creatorcontrib>Gething, Mary Jane H.</creatorcontrib><creatorcontrib>Davidson, Barrie E.</creatorcontrib><title>The Subunit Structure of Lactate Dehydrogenase from Streptococcus cremoris US3</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>1
Lactate dehydrogenase from Streptococcus cremoris US3, which has a molecular weight in solution of 140000, was found by dodecylsulphate‐gel electrophoresis to have a minimum molecular weight of 37000. It is, therefore, a tetramer.
2
Approximately 40 tryptic peptides were obtained by fingerprinting and in conjunction with the amino acid composition this indicates that the subunits are similar and probably identical.
3
There is one thiol group per subunit.
4
p‐Chloromercuribenzoate inhibits the enzyme.</description><subject>Amino Acids - analysis</subject><subject>Benzoates</subject><subject>Chloromercuribenzoates</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Chromatography, Gel</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fructosephosphates</subject><subject>Indicators and Reagents</subject><subject>L-Lactate Dehydrogenase - analysis</subject><subject>L-Lactate Dehydrogenase - antagonists & inhibitors</subject><subject>L-Lactate Dehydrogenase - isolation & purification</subject><subject>Macromolecular Substances</subject><subject>Molecular Weight</subject><subject>NAD</subject><subject>Nitro Compounds</subject><subject>Peptides - analysis</subject><subject>Protein Denaturation - drug effects</subject><subject>Sodium Dodecyl Sulfate</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Staining and Labeling</subject><subject>Streptococcus - enzymology</subject><subject>Trypsin</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1972</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE1PwkAQhjdGg4j-BJPGg7fW_aLtejGKoCZED4XzZrs7lRLK4m4b4d_bhoa7c5nJvO985EHojuCItPGwjghnNCSYsYiIhEZ1jinBPNqfoeFJOkdDjAkPqRjHl-jK-zXGOBZxMkADTiijCRmiz8UKgqzJm21ZB1ntGl03DgJbBHOla1VD8Aqrg3H2G7bKQ1A4W3U-2NVWW60bH2gHlXWlD5YZu0YXhdp4uOnzCC1n08XkPZx_vX1Mnueh5pSmoU6wUonRKTYCQywoY6T9Fahp-zmnChQTBrhpC6NiIrAaq5SbMUt0XsTARuj-uHfn7E8DvpZV6TVsNmoLtvEyJUksEsFa4-PRqJ313kEhd66slDtIgmUHU65lR0x2xGQHU_Yw5b4dvu2vNHkF5jTa02v1p6P-W27g8I_NcjZ9yRhP2R-Qg4Vf</recordid><startdate>197210</startdate><enddate>197210</enddate><creator>Dynon, Maria K.</creator><creator>Jago, G. Richard</creator><creator>Davidson, Barrie E.</creator><creator>Gething, Mary Jane H.</creator><creator>Davidson, Barrie E.</creator><general>Blackwell Publishing Ltd</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>7X8</scope></search><sort><creationdate>197210</creationdate><title>The Subunit Structure of Lactate Dehydrogenase from Streptococcus cremoris US3</title><author>Dynon, Maria K. ; Jago, G. Richard ; Davidson, Barrie E. ; Gething, Mary Jane H. ; Davidson, Barrie E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4228-c70aa7dc80d90e692331001e2d0aab42aea39de4daeada6190a5a84d537cbf6e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1972</creationdate><topic>Amino Acids - analysis</topic><topic>Benzoates</topic><topic>Chloromercuribenzoates</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Chromatography, Gel</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fructosephosphates</topic><topic>Indicators and Reagents</topic><topic>L-Lactate Dehydrogenase - analysis</topic><topic>L-Lactate Dehydrogenase - antagonists & inhibitors</topic><topic>L-Lactate Dehydrogenase - isolation & purification</topic><topic>Macromolecular Substances</topic><topic>Molecular Weight</topic><topic>NAD</topic><topic>Nitro Compounds</topic><topic>Peptides - analysis</topic><topic>Protein Denaturation - drug effects</topic><topic>Sodium Dodecyl Sulfate</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Staining and Labeling</topic><topic>Streptococcus - enzymology</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dynon, Maria K.</creatorcontrib><creatorcontrib>Jago, G. Richard</creatorcontrib><creatorcontrib>Davidson, Barrie E.</creatorcontrib><creatorcontrib>Gething, Mary Jane H.</creatorcontrib><creatorcontrib>Davidson, Barrie 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>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dynon, Maria K.</au><au>Jago, G. Richard</au><au>Davidson, Barrie E.</au><au>Gething, Mary Jane H.</au><au>Davidson, Barrie E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Subunit Structure of Lactate Dehydrogenase from Streptococcus cremoris US3</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1972-10</date><risdate>1972</risdate><volume>30</volume><issue>2</issue><spage>348</spage><epage>353</epage><pages>348-353</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>1
Lactate dehydrogenase from Streptococcus cremoris US3, which has a molecular weight in solution of 140000, was found by dodecylsulphate‐gel electrophoresis to have a minimum molecular weight of 37000. It is, therefore, a tetramer.
2
Approximately 40 tryptic peptides were obtained by fingerprinting and in conjunction with the amino acid composition this indicates that the subunits are similar and probably identical.
3
There is one thiol group per subunit.
4
p‐Chloromercuribenzoate inhibits the enzyme.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>4123271</pmid><doi>10.1111/j.1432-1033.1972.tb02104.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 1972-10, Vol.30 (2), p.348-353 |
| issn | 0014-2956 1432-1033 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_81769793 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Benzoates Chloromercuribenzoates Chromatography, DEAE-Cellulose Chromatography, Gel Electrophoresis, Polyacrylamide Gel Fructosephosphates Indicators and Reagents L-Lactate Dehydrogenase - analysis L-Lactate Dehydrogenase - antagonists & inhibitors L-Lactate Dehydrogenase - isolation & purification Macromolecular Substances Molecular Weight NAD Nitro Compounds Peptides - analysis Protein Denaturation - drug effects Sodium Dodecyl Sulfate Spectrophotometry, Ultraviolet Staining and Labeling Streptococcus - enzymology Trypsin |
| title | The Subunit Structure of Lactate Dehydrogenase from Streptococcus cremoris US3 |
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