By Paul D. Boyer (Eds.)
Content material: entrance hide; The Enzymes: Hydrolysis; Copyright web page; Contents; checklist of individuals; Preface; Contents of different Volumes; bankruptcy 1. The Hydrolysis of Sulfate Esters; bankruptcy 2. Arylsulfatases; bankruptcy three. Carboxylic Ester Hydrolases; bankruptcy four. Phospholipases; bankruptcy five. Acetylcholinesterase; bankruptcy 6. Plant and Animal Amylases; bankruptcy 7. Glycogen and Starch Debranching Enzymes; bankruptcy eight. Bacterial and mildew Amylases; bankruptcy nine. Cellulases; bankruptcy 10. Yeast and Neurospora lnvertases; bankruptcy eleven. Hyaluronidases; bankruptcy 12. Neuraminidases; bankruptcy thirteen. Phage Lysozyme and different Lytic Enzymes. bankruptcy 14. AconitaseChapter 15. ß-Hydroxydecanoyl Thioester Dehydrase; bankruptcy sixteen. Dehydration in Nucleotide-Linked Deoxysugar Synthesis; bankruptcy 17. Dehydrations Requiring nutrition B12 Coenzyme; bankruptcy 18. Enolase; bankruptcy 19. Fumarase and Crotonase; bankruptcy 20. 6-Phosphogluconic and similar Dehydrases; bankruptcy 21. Carbonic Anhydrase; writer Index; topic Index
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Extra resources for The Enzymes, Vol V: Hydrolysis (Sulfate Esters, Carboxyl Esters, Glycosides), Hydration, 3rd Edition
21 23 28 27 37 39 39 I. 1) are the best known of the sulfatases. Two representatives have been obtained as homogeneous proteins and others have been highly purified but, despite a considerable amount of information on the physical, chemical, and enzymological properties of these enzymes, a full understanding of the action of any one of them is remote. The present discussion will be restricted to those enzymes which have been significantly purified. More general topics have already been considered in Chapter 1 by Roy, this volume.
Chem. Soc. Japan 21, 267 (1957). 10. T. Harada and B. Spencer, BJ 82, 148 (1962). 11. A. B. Roy, BJ 68, 519 (1958); Australian J . Ezptl. B i d . Med. Sci. 41, 331 (1963). 4 A. B. ROT on the membrane system (Id). They have not been obtained in solution, and they arc always accompanied by steroid sulfatases: indirect evidence (see below) suggests that the latter are distinct from the arylsulfatases, but this has not been proved. The function of the arylsulfatases in animals is unknown. 2. Type II Arylsulfatases Type I1 arylsulfatases are found principally in animal tissues, where they are very widespread (2, 111, and only one example is known from microorganisms, that from Proteus vulgaris (IS).
Molar concentrations are in terms of the monomer. 30. A. B. Roy, BJ 55, 653 (1953); Ezperientiu 13, 32 (1957). 31. S. 0. Andersen, Acta Chem. Scand. 13, 884 and 1671 (1959). 2. 3. 14 pg/ml) at pH 5 and 37". 01% bovine serum albumin (stirred). the situation is further complicated by the surface denaturation which occurs when dilute solutions (< 5 pg/ml) of the enzyme are stirred, as during assays in the pH stat. 01% bovine serum albumin present in all assays. Examples of typical progress curves are shown in Fig.