Usability of Geopolymers for Oil Well Cementing Applications: Reaction Mechanisms, Pumpability, and Properties

Author(s):  
Mahmoud Khalifeh ◽  
Helge Hodne ◽  
Arild Saasen ◽  
Obara Integrity ◽  
Ekom I. Eduok
Keyword(s):  
Clay Minerals ◽  
1998 ◽  
Vol 33 (4) ◽  
pp. 539-546 ◽  
Author(s):  
P. A. Schroeder ◽  
A. A. McLain

AbstractFixed nitrogen in illite-smectites (I-S) has been measured for Miocene shales from a Gulf of Mexico oil well. Fixed N values for the <0.2 µm fraction increase with depth from 150 ppm (1000 m) to a maximum of 360 ppm (3841 m). This increase is coincident with illitization from 41% I in I-S to 75% I in I-S. Below 3841 m, fixed N values decrease to 190 ppm (4116 m) while I-S is maintained with a slight increase from 77 to 82%. The changes in fixed N with increasing illitization are consistent with the notion that illitization proceeds via both transformation and dissolution/ precipitation reaction mechanisms. The trend of decreasing fixed N in illitic I-S is compatible with surface-controlled crystal growth and Ostwald ripening mechanisms for illitization. The trend may also be linked to the timing of maximum NH] release from kerogen maturation during oil generation. The changing rate of NH+4 liberation from organic matter and multiple illitization reaction mechanisms can result in complex N geochemical cycling pathways throughout early diagenesis to metamorphism.


Author(s):  
Jeff Gelles

Mechanoenzymes are enzymes which use a chemical reaction to power directed movement along biological polymer. Such enzymes include the cytoskeletal motors (e.g., myosins, dyneins, and kinesins) as well as nucleic acid polymerases and helicases. A single catalytic turnover of a mechanoenzyme moves the enzyme molecule along the polymer a distance on the order of 10−9 m We have developed light microscope and digital image processing methods to detect and measure nanometer-scale motions driven by single mechanoenzyme molecules. These techniques enable one to monitor the occurrence of single reaction steps and to measure the lifetimes of reaction intermediates in individual enzyme molecules. This information can be used to elucidate reaction mechanisms and determine microscopic rate constants. Such an approach circumvents difficulties encountered in the use of traditional transient-state kinetics techniques to examine mechanoenzyme reaction mechanisms.


Author(s):  
A. Angel ◽  
K. Miller ◽  
V. Seybold ◽  
R. Kriebel

Localization of specific substances at the ultrastructural level is dependent on the introduction of chemicals which will complex and impart an electron density at specific reaction sites. Peroxidase-antiperoxidase(PAP) methods have been successfully applied at the electron microscopic level. The PAP complex is localized by addition of its substrate, hydrogen peroxide and an electron donor, usually diaminobenzidine(DAB). On oxidation, DAB forms an insoluble polymer which is able to chelate with osmium tetroxide becoming electron dense. Since verification of reactivity is visual, discrimination of reaction product from osmiophillic structures may be difficult. Recently, x-ray microanalysis has been applied to examine cytochemical reaction precipitates, their distribution in tissues, and to study cytochemical reaction mechanisms. For example, immunoreactive sites labelled with gold have been ascertained by means of x-ray microanalysis.


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