Title: The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme
Abstract: European Journal of BiochemistryVolume 14, Issue 2 p. 289-300 Free Access The Isolation and Crystallization of Yeast and Rabbit Liver Triose Phosphate Isomerase and a Comparative Characterization with the Rabbit Muscle Enzyme Wolfgang K. G. Krietsch, Wolfgang K. G. Krietsch Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorPeter G. Pentchev, Peter G. Pentchev Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorHelgard Klingenbürg, Helgard Klingenbürg Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorThomas Hofstätter, Thomas Hofstätter Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorTheodor Bücher, Theodor Bücher Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this author Wolfgang K. G. Krietsch, Wolfgang K. G. Krietsch Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorPeter G. Pentchev, Peter G. Pentchev Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorHelgard Klingenbürg, Helgard Klingenbürg Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorThomas Hofstätter, Thomas Hofstätter Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this authorTheodor Bücher, Theodor Bücher Institut für Physiologische Chemie und Physikalische Biochemie der UniversitätBRD-8000 München 15, Goethestraße 33, GermanySearch for more papers by this author First published: June 1970 https://doi.org/10.1111/j.1432-1033.1970.tb00289.xCitations: 77AboutSectionsPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL 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. Unusual Abbreviations pCMB para-chloromercuribenzoate DTNB 5,5′-dithiobis(2-nitrobenzoic acid) Enzymes Triose phosphate isomerase (EC 5.3.1.1) glycerol phosphate dehydrogenase (EC 1.1.1.8) d-glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) aldolase (EC 4.1.2.7) phosphoglycerate kinase (EC 2.7.1.31) pyruvic kinase (EC 2.7.1.40) lactic dehydrogenase (EC 1.1.1.27) enolase (EC 4.2.1.11) REFERENCES 1 Meyerhof, O., and Kiessling, W., Biochem. Z. 279 (1935) 40. 2 Meyer-Arendt, E., Beisenherz, G., and Bücher, Th., Naturwissenschaften, 40 (1953) 59. 3 Czok, R., and Bücher, Th., Advan. 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