By Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje Chang (eds.)
Springer instruction manual of Enzymes offers information on enzymes sufficiently good characterised. It deals concise and entire descriptions of a few 5,000 enzymes and their program components. information sheets are prepared of their EC-Number series and the volumes themselves are prepared based on enzyme classes.
This new, moment variation displays enormous development in enzymology: many enzymes are newly categorized or reclassified. each one access is correlated with references and a number of resource organisms. New datafields are created: software and engineering (for the homes of enzymes the place the series has been changed). the entire volume of fabric inside the guide has greater than doubled in order that the whole moment variation contains 39 volumes in addition to a Synonym Index. furthermore, beginning in 2009, all newly categorised enzymes are taken care of in complement Volumes.
Springer guide of Enzymes is a perfect resource of knowledge for researchers in biochemistry, biotechnology, natural and analytical chemistry, and foodstuff sciences, in addition to for medicinal applications.
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Extra info for Class 2 • Transferases IX: EC 126.96.36.199–188.8.131.52
The Enzymes, 3rd. Ed. : The effect of Mg 2+ on the Ca 2 + -binding properties of non-activated phosphorylase kinase. Eur. J. : Identification of the Ca 2 + -dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. ; Nishizuka, Y: Liver glycogen phosphorylase kinase. Partial purification and characterization. J. Biol. : Liver phosphorylase b kinase. Cyclic-AMP-mediated activation and properties of the partially purified rat-liver enzyme. Eur. J. : Chemical and regulatory properties of phosphorylase kinase and cyclic AMP-dependent protein kinase.
J. Biol. : Liver phosphorylase b kinase. Cyclic-AMP-mediated activation and properties of the partially purified rat-liver enzyme. Eur. J. : Chemical and regulatory properties of phosphorylase kinase and cyclic AMP-dependent protein kinase. Adv. Enzymol. Relat. Areas Mol. : Purification and properties of the cardiac isoenzyme of phosphorylase kinase. J. Biol. : Isolation and properties of the catalytically active y subunit of phosphorylase b kinase. J. Biol. : Phosphorylase kinase from dogfish skeletal muscle.
Biochem. : Synergistic activation by Ca 2+ and Mg 2+ as the primary cause for hysteresis in the phosphorylase kinase reactions. J. Biol. : Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active a y 8 and y 6 complexes. J. Biol. : Rabbit skeletal muscle phosphorylase kinase. Interactions between subunits and influence of calmodulin on different complexes. J. Biol. : Purification of rat liver phosphorylase kinase. J. Biol. : Multiple activities on phosphorylase kinase.