Pressure cycling reactor and methods of controlling reactions us

Chemical apparatus and process disinfecting – deodorizing – preser – Analyzer – structured indicator – or manipulative laboratory... – Means for analyzing liquid or solid sample

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435 6, 435 911, 435 912, 436 94, 536 231, 422 99, 422102, 422103, C12Q 168, G01N 700, B01L 1100, C07H 2104

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06036923&

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BRIEF SUMMARY
FIELD OF THE INVENTION

The invention is in the general field of apparatus for containing and conducting chemical reactions. The invention also provides methods of using the apparatus to provide control over one or more chemical reactions in a series.


BACKGROUND OF THE INVENTION

Chemical reactions encompass molecular interactions such as the formation and cleavage of covalent bonds and ionic bonds; the association or dissociation of two or more chemical compounds; and changes in primary, secondary, tertiary, or quaternary structure. Chemical reactions include nonenzymatic and enzymatic reactions. Whether or not enzymes are present, a chemical reaction is usually made of several mechanistic steps or molecular interactions, including conformational changes, transition state formation, electron or proton donation/acceptance, and electron rearrangement. Typically, a series of chemical reactions provides a useful chemical product.
For example, in molecular biology, nested sets of deletions are used to create site-directed mutants which are used to probe the function of DNA segments in both structural and regulatory gene sequences. A collection of nested deletions within a gene allows the fine mapping of regions such as enhancers, promoters, and termination sites which are necessary for regulatory functions; and regions having structural function, such as those defining domains within proteins. It is desirable to create deletions which vary only slightly from each other, for example, by 10-20 base pairs. Existing methods for generating nested sets of deletions digest double stranded DNA with nucleases including restriction endonucleases, Bal31, pancreatic DNase I (DNase I), and Exonuclease III (Exo III).
Restriction endonucleases are used to partially digest a DNA template which contains multiple sites for a given restriction endonuclease. This method requires prior knowledge of restriction sites within a DNA template. Because restriction sites are not randomly distributed throughout a DNA template, many DNA templates will not contain sufficient or properly spaced restriction enzyme sites to generate a useful set of deletion mutants. This is particularly problematic when the mutants are intended to delineate the boundary of regulatory domains.
Turning to another endonuclease, Bal 31 digests double stranded linear DNA from both the 5' and 3' termini. To create a set of unidirectional mutants, a double stranded DNA template (plasmid, phage, or replicative form of M13) is linearized with a restriction enzyme which cleaves at one end of the target sequence. The linearized DNA is incubated with Bal 31. Varying time and the amount of enzyme respectively control the extent of digestion and the rate of digestion. Most commercial preparations of Bal 31 contain two distinct forms of the enzyme, a fast and a slow form, the latter being a proteolytic fragment of the former. The extent of digestion depends on the proportion of the two forms. Each batch of Bal 31 is therefore assayed to determine suitable digestion conditions.
Bal 31 is a processive enzyme which simultaneously degrades both the target DNA and the flanking vector DNA. Bal 31 activity varies with the primary structure of the DNA template; A-T rich regions are degraded faster than G-C rich regions. Recovery of the truncated target fragments and subcloning into an appropriate vector is required. The processive properties result in the generation of heterogeneous deletions. Bal 31 requires purification because it is inhibited by the presence of RNA.
Turning to a third enzyme, pancreatic DNase I will cut double stranded DNA templates at about the same location on both strands, in the presence of transition metal ions such as Mn.sup.2+ or Co.sup.2+. Incubation of closed circular DNA with DNase I generates a set of linear molecules which are cut at locations randomly dispersed throughout the target DNA. A portion of the starting material is never converted to the linear form. After a restriction enzyme cleaves at one end of the target sequence, the sequences are r

REFERENCES:
patent: 3750911 (1973-08-01), Ebner et al.
patent: 3901874 (1975-08-01), Hill et al.
patent: 4066868 (1978-01-01), Witkin et al.
patent: 4070008 (1978-01-01), Schlieckmann
patent: 4263406 (1981-04-01), Bostick et al.
patent: 4297323 (1981-10-01), Tetzlaff et al.
patent: 4412552 (1983-11-01), Kolbanovsky et al.
patent: 4636473 (1987-01-01), Kleinstreuer
patent: 4879132 (1989-11-01), Tsuchiya et al.
patent: 4987933 (1991-01-01), Mack et al.
patent: 5027902 (1991-07-01), Dickinson et al.
patent: 5403563 (1995-04-01), Crosbie et al.
patent: 5455175 (1995-10-01), Wittwer et al.
patent: 5478910 (1995-12-01), Russel et al.
patent: 5512462 (1996-04-01), Cheng
patent: 5658610 (1997-08-01), Bergman et al.
Robert B. Macgregor, Jr., "Reversible Inhibitiion of EcoRI with Elevated Pressure," Biochemical and Biophysical Research Communications, pp. 775-778 (1990).
Michels et al., "Pressure Dependence of Enzyme Catalysis," American Chemical Society, pp. 108-121 (1992).
K.R. Brower, "A Method for Measuring the Activation Volumes of Fast Reversible Reactions. The Ferric Thiocyanate Complex," Journal of American Chemical Society, pp. 5401-5403 (1968).
Miller et al., "High Pressure-Temperature Bioreactor: Assays of Thermostable Hydrogenase with Fiber Optics," Biotechnology and Bioengineering, pp. 1015-1021 (1989).
Michels et al., "Pressure-Enhanced Activity and Stability of a Hyperthermophilic Protease from a Deep-Sea Methanogen", Applied and Environmental Microbiology, vol. 63, No. 10, pp. 3985-3991, (1997).
Kunugi et al., "Effect of Pressure on Plant Endonuclease Reactions", Sixteenth Symposium on Nucelic Acids Chemistry, No. 21, pp. 133-134, (1989).
Kunugi, "Use of Pressure for Enzyme Reactions", Tanpakushitsu Kakusan Koso, 34(2), 113-118, (1989).
Clegg et al., "Communications to the Editor," Biopolymers, 14:883-887, 1975.
Dreyfus et al., "Effect of Hydrostatic Pressure on the Mitochondrial ATP Synthase," Biochemistry, Am. Chem. Soc., 27:6704-6710, 1988.
Landau, "Hydrostatic Pressure on the Biosynthesis of Macromolecules," [Book], Chapter 2, pp. 45-49, [year].
Mozhaev et al., "Exploiting the effects of high hydrostatic pressure in biotechnological applications," Tibtech, 12:493-501, 1994.
Paladini, Jr. , et al., "Pressure-Induced Reversible Dissociation of Enolase," Biochemistry, Am. Chem. Soc., 20(9):2587-2593, 1981.

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