[Extraction of crystalline L-threonine(serine)-dehydratase from rat liver]. 1979

B V Pokrovskiĭ

Isolation on a preparative scale of crystalline pyridoxal phosphate-dependent threonine dehydratase (responsible for threonine deamination) from rat liver tissue is described. The enzyme was purified by stepwise salting out with (NH4)2SO4, two precipitations with acetone, gel filtration through Sephadex G-25, chromatography on DEAE cellulose, repricipitation with ammonium sulfate and crystallization. The ratio of threonine to serine dehydratase activities was altered only slightly through all the steps of the purification procedure. Both enzymes proved to be similar in their chromatographic properties; this suggests that a single enzyme is responsible for dehydrative deamination of both hydroxyamino acids in rat liver tissue. Stability of the enzyme preparations was distinctly increased after DEAE cellulose chromatography. The yield of crystalline threonine (serine) dehydratase was about 3%; the enzyme was purified 1500-1800-fold.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012695 L-Serine Dehydratase A PYRIDOXAL-phosphate containing enzyme that catalyzes the dehydration and deamination of L-serine to form pyruvate. This enzyme was formerly listed as EC 4.2.1.13. Serine Deaminase,Serine Dehydratase,L-Serine Ammonia-Lyase,Serine-Threonine Dehydratase,Ammonia-Lyase, L-Serine,Deaminase, Serine,Dehydratase, L-Serine,Dehydratase, Serine,Dehydratase, Serine-Threonine,L Serine Ammonia Lyase,L Serine Dehydratase,Serine Threonine Dehydratase
D013913 Threonine Dehydratase A pyridoxal-phosphate protein that catalyzes the deamination of THREONINE to 2-ketobutyrate and AMMONIA. The role of this enzyme can be biosynthetic or biodegradative. In the former role it supplies 2-ketobutyrate required for ISOLEUCINE biosynthesis, while in the latter it is only involved in the breakdown of threonine to supply energy. This enzyme was formerly listed as EC 4.2.1.16. Threonine Deaminase,Threonine Dehydrase,Threonine Ammonia-Lyase,Ammonia-Lyase, Threonine,Deaminase, Threonine,Dehydrase, Threonine,Dehydratase, Threonine,Threonine Ammonia Lyase
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus
D066298 In Vitro Techniques Methods to study reactions or processes taking place in an artificial environment outside the living organism. In Vitro Test,In Vitro Testing,In Vitro Tests,In Vitro as Topic,In Vitro,In Vitro Technique,In Vitro Testings,Technique, In Vitro,Techniques, In Vitro,Test, In Vitro,Testing, In Vitro,Testings, In Vitro,Tests, In Vitro,Vitro Testing, In

Related Publications

B V Pokrovskiĭ
October 1978, Biokhimiia (Moscow, Russia),
B V Pokrovskiĭ
November 1969, Journal of biochemistry,
B V Pokrovskiĭ
October 1993, Protein expression and purification,
B V Pokrovskiĭ
August 1970, Zeitschrift fur die gesamte experimentelle Medizin einschliesslich experimentelle Chirurgie,
B V Pokrovskiĭ
September 1973, Biochimica et biophysica acta,
B V Pokrovskiĭ
January 1982, Progress in clinical and biological research,
Copied contents to your clipboard!