scholarly journals Fungal Cellulases XVI. Alkane-1, O-Diols As Acceptors for the ?-Glucosidase of Stachybotrys Atra

1966 ◽  
Vol 19 (5) ◽  
pp. 919
Author(s):  
MA Jermyn
Keyword(s):  
Partial Reaction ◽  
Water Complex ◽  
Effects Of Ph ◽  
Stachybotrys Atra ◽  
Kinetics Of

Using hexane-l,6-diol as an exemplar, methods are developed for estimating the kinetics of the reaction of enzyme and phenyl ,B-D-glucopyranoside with an added acceptor. The effects of pH on the rate of decomposition of the enzymeglucoside- hexanediol complex and on the Micl;laelis constant of the partial reaction of enzyme-hexanediol with glucoside are considerably different from those for the water complex. Some less certain deductions are also made for the reaction of enzyme with butane-l,4-diol and p-nitrophenyl ,B-D-glucopyranoside.

Effect of pH and inhibitors on beta-amyloid fibril assembly

1996 ◽  
Vol 54 ◽  
pp. 752-753
Author(s):  
Beverly E. Maleeff ◽  
Timothy K. Hart ◽  
Stephen J. Wood ◽  
Ronald Wetzel
Keyword(s):  
Amyloid Fibril ◽  
Peptide Fragment ◽  
Hydrophobic Peptides ◽  
Amyloid Fibril Formation ◽  
Effects Of Ph ◽  
Severity Of The Disease ◽  
Kinetics Of ◽  
The Brain

Alzheimer's disease is characterized post-mortem in part by abnormal extracellular neuritic plaques found in brain tissue. There appears to be a correlation between the severity of Alzheimer's dementia in vivo and the number of plaques found in particular areas of the brain. These plaques are known to be the deposition sites of fibrils of the protein β-amyloid. It is thought that if the assembly of these plaques could be inhibited, the severity of the disease would be decreased. The peptide fragment Aβ, a precursor of the p-amyloid protein, has a 40 amino acid sequence, and has been shown to be toxic to neuronal cells in culture after an aging process of several days. This toxicity corresponds to the kinetics of in vitro amyloid fibril formation. In this study, we report the biochemical and ultrastructural effects of pH and the inhibitory agent hexadecyl-N-methylpiperidinium (HMP) bromide, one of a class of ionic micellar detergents known to be capable of solubilizing hydrophobic peptides, on the in vitro assembly of the peptide fragment Aβ.

Effects of pH on kinetics of binding of mRNA-cap analogs by translation initiation factor eIF4E

2003 ◽  
Vol 31 (8) ◽  
pp. 608-616 ◽  
Author(s):  
M. Długosz ◽  
E. Błachut-Okrasińska ◽  
E. Bojarska ◽  
E. Darżynkiewicz ◽  
J. Antosiewicz
Keyword(s):  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Effects Of Ph ◽  
Kinetics Of

The Characteristics and Kinetic Equation of 4-CP Biodegradation by Fusarium sp. HJ01

2012 ◽  
Vol 554-556 ◽  
pp. 1925-1928 ◽  
Author(s):  
Ji Wu Li ◽  
Xiao Hong Zhu ◽  
Jun Ya Pan
Keyword(s):  
Carbon Source ◽  
Sole Carbon Source ◽  
Degradation Rate ◽  
Order Equation ◽  
First Order ◽  
Haldane Model ◽  
Effects Of Ph ◽  
Fusarium Sp ◽  
Ph Range ◽  
Kinetics Of

The stain of Fusarium sp. HJ01 used in 4-chlorophenol (4-CP) degradation was isolated in our laboratory. The effects of pH, temperature, 4-CP concentration, carbon source on 4-CP degradation rate were studied. It was concluded that Fusarium sp. HJ01 could grow with 4-CP as the sole carbon and energy source. 4-CP concentration of 100mg/L in the pH range of 4~10 and temperature range of 25°C~35°C could be degraded completely. The capacity of 4-CP degradation was effectively enhanced by the addiction of sucrose. The kinetics of 4-CP degradation could well accord with the Haldane model for 4-CP as the sole carbon source and with first order equation for added other sucrose.

scholarly journals Short Communications. A comparative study of some kinetic and spectral properties of guanidinated and native cytochrome c

1975 ◽  
Vol 147 (1) ◽  
pp. 175-177 ◽  
Author(s):  
T Brittain ◽  
C Greenwood
Keyword(s):  
Cytochrome C ◽  
Comparative Study ◽  
Spectral Properties ◽  
Visible Spectrum ◽  
Kinetic Properties ◽  
Chemically Modified ◽  
Effects Of Ph ◽  
Kinetics Of ◽  
Kinetics Of Reduction

An investigation of the spectral and some kinetic properties of a chemically modified cytochrome c is presented. The kinetics of reduction by chromous ion and ascorbate are shown to be unchanged from that of the native molecule, as are the kinetics of NO binding. The effects of pH on the visible spectrum are discussed in terms of a possible change in the pattern of co-ordination of the molecule with changing pH.

Effects of pH and acid anions on the dissolution kinetics of MgO

2008 ◽  
Vol 143 (1-3) ◽  
pp. 265-272 ◽  
Author(s):  
Alena Fedoročková ◽  
Pavel Raschman
Keyword(s):  
Dissolution Kinetics ◽  
Effects Of Ph ◽  
Kinetics Of

scholarly journals The combination of carbon monoxide–haem with apoperoxidase

1969 ◽  
Vol 114 (4) ◽  
pp. 719-724 ◽  
Author(s):  
Charles Phelps ◽  
Eraldo Antonini
Keyword(s):  
Activation Energy ◽  
Carbon Monoxide ◽  
Rate Constant ◽  
Binding Sites ◽  
Order Process ◽  
First Order ◽  
Effects Of Ph ◽  
Kinetics Of

1. Static titrations reveal an exact stoicheiometry between various haem derivatives and apoperoxidase prepared from one isoenzyme of the horseradish enzyme. 2. Carbon monoxide–protohaem reacts rapidly with apoperoxidase and the kinetics can be accounted for by a mechanism already applied to the reaction of carbon monoxide–haem derivatives with apomyoglobin and apohaemoglobin. 3. According to this mechanism a complex is formed first whose combination and dissociation velocity constants are 5×108m−1sec.−1 and 103sec.−1 at pH9·1 and 20°. The complex is converted into carbon monoxide–haemoprotein in a first-order process with a rate constant of 235sec.−1 for peroxidase and 364sec.−1 for myoglobin at pH9·1 and 20°. 4. The effects of pH and temperature were examined. The activation energy for the process of complex-isomerization is about 13kcal./mole. 5. The similarity in the kinetics of the reactions of carbon monoxide–haem with apoperoxidase and with apomyoglobin suggests structural similarities at the haem-binding sites of the two proteins.

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