Kinetic constants for the hydrolysis of aggrecan by the papaya proteinases and their relevance for chemonucleolysis
β Scribed by P.M. Dekeyser; D.J. Buttle; B. Devreese; J. Van Beeumen; J. Demeester; A. Lauwers
- Book ID
- 115709377
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 485 KB
- Volume
- 320
- Category
- Article
- ISSN
- 0003-9861
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Liquid chromatography and "C-n.m.r. spectroscopy have been used to isolate and characterize the fructo-oligosaccharides present in the juice of Jerusalem artichoke. Oligosaccharides having d.p. 2-7 were purified individually. A kinetic study was performed to determine the dependence of the acid
We have designed this study to determine various kinetic parameters of camel retinal membranebound acetylcholinesterase (AChE; EC 3.1.1.7) inhibition by carbamate insecticide lannate [methyl N-{{(methylamino)carbonyl}oxy} ethanimidothioate]. All these kinetic constants were derived by simple graphic
Kinetic results on the glucoamylase-catalysed hydrolysis of maltose and maltotriose, and glucose polymerization into maltose and isomaltose up to 450 g/L total sugar concentration are presented. Whereas the enzyme has a faster hydrolytic and synthetic activity on ~(1'4) than on a-(I -6) linkages, at
## Abstract Pseudoβfirstβorder rate constants (k~obs~) for pHβindependent hydrolysis of phthalimide (1), obtained at a constant total concentration of cetyltrimethylammonium bromide and hydroxide ([CTABr]~T~), 2.0 Γ 10^β4^ M 1, 0.02 M MOH (M^+^ = Li^+^, Na^+^ and K^+^) and various concentrations of