By Professor Dietmar Schomburg, Dr. Ida Schomburg (eds.)

Springer instruction manual of Enzymes offers info on enzymes sufficiently good characterised. It bargains concise and whole descriptions of a few 5,000 enzymes and their program components. info sheets are prepared of their EC-Number series and the volumes themselves are prepared in accordance with enzyme classes.

This new, moment version displays substantial development in enzymology: many enzymes are newly categorised or reclassified. each one access is correlated with references and a number of resource organisms. New datafields are created: program and engineering (for the houses of enzymes the place the series has been changed). the whole volume of fabric inside the instruction manual has greater than doubled in order that the total moment variation includes 39 volumes in addition to a Synonym Index. additionally, beginning in 2009, all newly categorized enzymes are handled in complement Volumes.

Springer guide of Enzymes is a perfect resource of knowledge for researchers in biochemistry, biotechnology, natural and analytical chemistry, and nutrients sciences, in addition to for medicinal applications.

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8, 15, 20> (<20> ? * 23000-24000, SDS-PAGE [44]; <8> ? * 18500, SDSPAGE, isozyme I and II [33]; <15> ? * 22000, SDS-PAGE [38]) [33, 38, 44] dimer <6, 8, 24, 25, 33, 48> (<48> 2 * 19000, recombinant enzyme, SDSPAGE, mass spectroscopy [89]; <6> 2 * 58000, isoform IIa, SDS-PAGE [26]; <6> 2 * 56700, bifunctional enzyme: thymidylate synthase-dihydrofolate reductase, SDS-PAGE [2,25]; <24> 2 * 56400, methotrexate-resistant, each subunit is a bifunctional thymidylate synthase-dihydrofolate reductase, SDSPAGE [48]; <25> 2 * 50000, thymidylate synthase and dihydrofolate reductase cannot be dissociated from each other, SDS-PAGE [49]; <33> isozymes type I [1]) [1, 2, 25, 26, 48, 49, 84, 89] monomer <1-3, 5, 7, 8, 11, 13, 14, 18, 19, 21, 22, 30, 32-34> (<34> 1 * 20000, SDS-PAGE [77]; <32> 1 * 24000, recombinant enzyme, SDS-PAGE [75]; <22> 1 * 173000, both forms, SDS-PAGE [46]; <19> 1 * 25000, recombinant from E.

18500, SDSPAGE, isozyme I and II [33]; <15> ? * 22000, SDS-PAGE [38]) [33, 38, 44] dimer <6, 8, 24, 25, 33, 48> (<48> 2 * 19000, recombinant enzyme, SDSPAGE, mass spectroscopy [89]; <6> 2 * 58000, isoform IIa, SDS-PAGE [26]; <6> 2 * 56700, bifunctional enzyme: thymidylate synthase-dihydrofolate reductase, SDS-PAGE [2,25]; <24> 2 * 56400, methotrexate-resistant, each subunit is a bifunctional thymidylate synthase-dihydrofolate reductase, SDSPAGE [48]; <25> 2 * 50000, thymidylate synthase and dihydrofolate reductase cannot be dissociated from each other, SDS-PAGE [49]; <33> isozymes type I [1]) [1, 2, 25, 26, 48, 49, 84, 89] monomer <1-3, 5, 7, 8, 11, 13, 14, 18, 19, 21, 22, 30, 32-34> (<34> 1 * 20000, SDS-PAGE [77]; <32> 1 * 24000, recombinant enzyme, SDS-PAGE [75]; <22> 1 * 173000, both forms, SDS-PAGE [46]; <19> 1 * 25000, recombinant from E.

Pyrroline-5-carboxylate reductase in Chlorella autotrophica and Chlorella saccharophila in relation to osmoregulation. : Cloning and physical characterization of the l-proline catabolism gene cluster of Aspergillus nidulans. Mol. ; Hagedorn, C. : Proline metabolism in N2 -fixing root nodules: energy transfer and regulation of purine synthesis. Proc. Natl. Acad. Sci. : Demonstration of a NADPH-linked D1 -pyrroline-5-carboxylate-proline shuttle in a cell-free rat liver system. Biochim. Biophys.

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