The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme
Triose phosphate isomerase was isolated from brewer's yeast and rabbit liver and was obtained in crystalline form. Chemical, physical and kinetic properties were compared to rabbit muscle triose phosphate isomerase. 1 The molecular weight of all three enzymes is in the range of 56000 to 60000....
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| Veröffentlicht in: | European journal of biochemistry 1970-06, Vol.14 (2), p.289-300 |
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| container_title | European journal of biochemistry |
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| creator | Krietsch, Wolfgang K. G. Pentchev, Peter G. Klingenbürg, Helgard Hofstätter, Thomas Bücher, Theodor |
| description | Triose phosphate isomerase was isolated from brewer's yeast and rabbit liver and was obtained in crystalline form. Chemical, physical and kinetic properties were compared to rabbit muscle triose phosphate isomerase.
1
The molecular weight of all three enzymes is in the range of 56000 to 60000. In dodecyl sulfate or as modified maleylated protein, the enzymes dissociate into two polypeptide chains each having a molecular weight in the range of 24000 to 29000.
2
The rabbit muscle and liver enzymes appear to be indistinguishable in terms of their amino acid composition, electrophoretic mobility, kinetic properties, inhibition sensitivity, pH optimum, molecular weight and N‐terminal amino acid (alanine).
3
The yeast enzyme, on the other hand, was found different in the following respects; it has a several fold lower content of sulfur amino acids, is highly resistant to inactivation through photooxidation as well as sulfhydryl and alkylating agents. Furthermore, it contains different N‐terminal amino acids (valine and alanine) and has kinetic properties differing from those of the rabbit enzymes.
4
The crystalline liver and muscle enzymes could be resolved into three distinct electrophoretic forms in starch and polyacrylamide gels. The possible interpretation of the multiple forms in terms of hybrids or conformers is discussed. |
| doi_str_mv | 10.1111/j.1432-1033.1970.tb00289.x |
| format | Article |
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1
The molecular weight of all three enzymes is in the range of 56000 to 60000. In dodecyl sulfate or as modified maleylated protein, the enzymes dissociate into two polypeptide chains each having a molecular weight in the range of 24000 to 29000.
2
The rabbit muscle and liver enzymes appear to be indistinguishable in terms of their amino acid composition, electrophoretic mobility, kinetic properties, inhibition sensitivity, pH optimum, molecular weight and N‐terminal amino acid (alanine).
3
The yeast enzyme, on the other hand, was found different in the following respects; it has a several fold lower content of sulfur amino acids, is highly resistant to inactivation through photooxidation as well as sulfhydryl and alkylating agents. Furthermore, it contains different N‐terminal amino acids (valine and alanine) and has kinetic properties differing from those of the rabbit enzymes.
4
The crystalline liver and muscle enzymes could be resolved into three distinct electrophoretic forms in starch and polyacrylamide gels. The possible interpretation of the multiple forms in terms of hybrids or conformers is discussed.</description><identifier>ISSN: 0014-2956</identifier><identifier>EISSN: 1432-1033</identifier><identifier>DOI: 10.1111/j.1432-1033.1970.tb00289.x</identifier><identifier>PMID: 5506172</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acids - analysis ; Animals ; Chemical Phenomena ; Chemistry ; Chromatography, Gel ; Crystallization ; Detergents ; Electrophoresis ; Glycerophosphates ; Hydrogen-Ion Concentration ; Isomerases - analysis ; Isomerases - antagonists & inhibitors ; Isomerases - isolation & purification ; Kinetics ; Light ; Liver - enzymology ; Maleates ; Molecular Weight ; Muscles - enzymology ; Oxidation-Reduction ; Photochemistry ; Rabbits ; Rats ; Saccharomyces - enzymology ; Sulfhydryl Compounds - analysis ; Sulfuric Acids ; Trioses ; Tryptophan - analysis ; Ultracentrifugation</subject><ispartof>European journal of biochemistry, 1970-06, Vol.14 (2), p.289-300</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4229-c1e29651ef88714cfc948b9879d6003c950d20b168566254374a28f55d37ad113</citedby><cites>FETCH-LOGICAL-c4229-c1e29651ef88714cfc948b9879d6003c950d20b168566254374a28f55d37ad113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/5506172$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Krietsch, Wolfgang K. G.</creatorcontrib><creatorcontrib>Pentchev, Peter G.</creatorcontrib><creatorcontrib>Klingenbürg, Helgard</creatorcontrib><creatorcontrib>Hofstätter, Thomas</creatorcontrib><creatorcontrib>Bücher, Theodor</creatorcontrib><title>The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme</title><title>European journal of biochemistry</title><addtitle>Eur J Biochem</addtitle><description>Triose phosphate isomerase was isolated from brewer's yeast and rabbit liver and was obtained in crystalline form. Chemical, physical and kinetic properties were compared to rabbit muscle triose phosphate isomerase.
1
The molecular weight of all three enzymes is in the range of 56000 to 60000. In dodecyl sulfate or as modified maleylated protein, the enzymes dissociate into two polypeptide chains each having a molecular weight in the range of 24000 to 29000.
2
The rabbit muscle and liver enzymes appear to be indistinguishable in terms of their amino acid composition, electrophoretic mobility, kinetic properties, inhibition sensitivity, pH optimum, molecular weight and N‐terminal amino acid (alanine).
3
The yeast enzyme, on the other hand, was found different in the following respects; it has a several fold lower content of sulfur amino acids, is highly resistant to inactivation through photooxidation as well as sulfhydryl and alkylating agents. Furthermore, it contains different N‐terminal amino acids (valine and alanine) and has kinetic properties differing from those of the rabbit enzymes.
4
The crystalline liver and muscle enzymes could be resolved into three distinct electrophoretic forms in starch and polyacrylamide gels. The possible interpretation of the multiple forms in terms of hybrids or conformers is discussed.</description><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Chromatography, Gel</subject><subject>Crystallization</subject><subject>Detergents</subject><subject>Electrophoresis</subject><subject>Glycerophosphates</subject><subject>Hydrogen-Ion Concentration</subject><subject>Isomerases - analysis</subject><subject>Isomerases - antagonists & inhibitors</subject><subject>Isomerases - isolation & purification</subject><subject>Kinetics</subject><subject>Light</subject><subject>Liver - enzymology</subject><subject>Maleates</subject><subject>Molecular Weight</subject><subject>Muscles - enzymology</subject><subject>Oxidation-Reduction</subject><subject>Photochemistry</subject><subject>Rabbits</subject><subject>Rats</subject><subject>Saccharomyces - enzymology</subject><subject>Sulfhydryl Compounds - analysis</subject><subject>Sulfuric Acids</subject><subject>Trioses</subject><subject>Tryptophan - analysis</subject><subject>Ultracentrifugation</subject><issn>0014-2956</issn><issn>1432-1033</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1970</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1u1DAUhS0EKkPLIyBZLNgl-Cd2bDaIRlNaaRBVOyxYWY7jKBkl48H2tJ2-CK9bpxO6xxtf3XPud6V7APiIUY7T-7zJcUFJhhGlOZYlymONEBEyf3gFFi_Sa7BACBcZkYy_Be9C2CCEuOTlCThhDHFckgX4u-4svApu0LF3W6i3Daz8IUQ9DP3jseda-NvqEJ_FG13XfYSr_s56uPa9CxZedy7sOh2fQaP1OvUmr4aVG3faJ8ydhVWXKhOt_8e972MHY1o_M3_sgxksXG4fD6M9A29aPQT7fv5Pwa-L5bq6zFY_v19V31aZKQiRmcGWSM6wbYUocWFaIwtRS1HKhiNEjWSoIajGXDDOCStoWWgiWsYaWuoGY3oKPh25O-_-7G2IauyDscOgt9btgxJFSTnBIhm_HI3GuxC8bdXO96P2B4WRmlJRGzWdXk2nV1Mqak5FPaThD_OWfT3a5mV0jiHpX4_6fT_Yw3-Q1cXy_DZV9AleNZ4v</recordid><startdate>197006</startdate><enddate>197006</enddate><creator>Krietsch, Wolfgang K. G.</creator><creator>Pentchev, Peter G.</creator><creator>Klingenbürg, Helgard</creator><creator>Hofstätter, Thomas</creator><creator>Bücher, Theodor</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>197006</creationdate><title>The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme</title><author>Krietsch, Wolfgang K. G. ; Pentchev, Peter G. ; Klingenbürg, Helgard ; Hofstätter, Thomas ; Bücher, Theodor</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4229-c1e29651ef88714cfc948b9879d6003c950d20b168566254374a28f55d37ad113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1970</creationdate><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Chromatography, Gel</topic><topic>Crystallization</topic><topic>Detergents</topic><topic>Electrophoresis</topic><topic>Glycerophosphates</topic><topic>Hydrogen-Ion Concentration</topic><topic>Isomerases - analysis</topic><topic>Isomerases - antagonists & inhibitors</topic><topic>Isomerases - isolation & purification</topic><topic>Kinetics</topic><topic>Light</topic><topic>Liver - enzymology</topic><topic>Maleates</topic><topic>Molecular Weight</topic><topic>Muscles - enzymology</topic><topic>Oxidation-Reduction</topic><topic>Photochemistry</topic><topic>Rabbits</topic><topic>Rats</topic><topic>Saccharomyces - enzymology</topic><topic>Sulfhydryl Compounds - analysis</topic><topic>Sulfuric Acids</topic><topic>Trioses</topic><topic>Tryptophan - analysis</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Krietsch, Wolfgang K. G.</creatorcontrib><creatorcontrib>Pentchev, Peter G.</creatorcontrib><creatorcontrib>Klingenbürg, Helgard</creatorcontrib><creatorcontrib>Hofstätter, Thomas</creatorcontrib><creatorcontrib>Bücher, Theodor</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>Krietsch, Wolfgang K. G.</au><au>Pentchev, Peter G.</au><au>Klingenbürg, Helgard</au><au>Hofstätter, Thomas</au><au>Bücher, Theodor</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1970-06</date><risdate>1970</risdate><volume>14</volume><issue>2</issue><spage>289</spage><epage>300</epage><pages>289-300</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><abstract>Triose phosphate isomerase was isolated from brewer's yeast and rabbit liver and was obtained in crystalline form. Chemical, physical and kinetic properties were compared to rabbit muscle triose phosphate isomerase.
1
The molecular weight of all three enzymes is in the range of 56000 to 60000. In dodecyl sulfate or as modified maleylated protein, the enzymes dissociate into two polypeptide chains each having a molecular weight in the range of 24000 to 29000.
2
The rabbit muscle and liver enzymes appear to be indistinguishable in terms of their amino acid composition, electrophoretic mobility, kinetic properties, inhibition sensitivity, pH optimum, molecular weight and N‐terminal amino acid (alanine).
3
The yeast enzyme, on the other hand, was found different in the following respects; it has a several fold lower content of sulfur amino acids, is highly resistant to inactivation through photooxidation as well as sulfhydryl and alkylating agents. Furthermore, it contains different N‐terminal amino acids (valine and alanine) and has kinetic properties differing from those of the rabbit enzymes.
4
The crystalline liver and muscle enzymes could be resolved into three distinct electrophoretic forms in starch and polyacrylamide gels. The possible interpretation of the multiple forms in terms of hybrids or conformers is discussed.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>5506172</pmid><doi>10.1111/j.1432-1033.1970.tb00289.x</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | European journal of biochemistry, 1970-06, Vol.14 (2), p.289-300 |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Animals Chemical Phenomena Chemistry Chromatography, Gel Crystallization Detergents Electrophoresis Glycerophosphates Hydrogen-Ion Concentration Isomerases - analysis Isomerases - antagonists & inhibitors Isomerases - isolation & purification Kinetics Light Liver - enzymology Maleates Molecular Weight Muscles - enzymology Oxidation-Reduction Photochemistry Rabbits Rats Saccharomyces - enzymology Sulfhydryl Compounds - analysis Sulfuric Acids Trioses Tryptophan - analysis Ultracentrifugation |
| title | The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme |
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