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|Original author(s)||Leslie Lamport|
|License||LaTeX Project Public License (LPPL)|
LaTeX (formatted as LaTeX, pronounced //, //, //, or //), is a document markup language and document preparation system for the TeX typesetting program. The term LaTeX refers only to the language in which documents are written, not to the editor application used to write those documents. In order to create a document in LaTeX, a .tex file must be created using some form of text editor. While most text editors can be used to create a LaTeX document, a number of editors have been created specifically for working with LaTeX.
LaTeX is widely used in academia. It is also used as the primary method of displaying formulas on Wikipedia. As a primary or intermediate format, e.g., translating DocBook and other XML-based formats to PDF, LaTeX is used because of the high quality of typesetting achievable by TeX. The typesetting system offers programmable desktop publishing features and extensive facilities for automating most aspects of typesetting and desktop publishing, including numbering and cross-referencing, tables and figures, page layout and bibliographies.
LaTeX is intended to provide a high-level language that accesses the power of TeX. LaTeX essentially comprises a collection of TeX macros and a program to process LaTeX documents. Because the TeX formatting commands are very low-level, it is usually much simpler for end-users to use LaTeX.
LaTeX was originally written in the early 1980s by Leslie Lamport at SRI International. The current version is LaTeX2e (styled as LaTeX2ε). LaTeX is free software and is distributed under the LaTeX Project Public License (LPPL).Template:MaTeX2e
LaTeX is based on the philosophy that authors should be able to focus on the content of what they are writing without being distracted by its visual presentation. In preparing a LaTeX document, the author specifies the logical structure using familiar concepts such as chapter, section, table, figure, etc., and lets the LaTeX system worry about the presentation of these structures. It therefore encourages the separation of layout from content while still allowing manual typesetting adjustments where needed. This is similar to the mechanism by which many word processors allow styles to be defined globally for an entire document or the use of Cascading Style Sheets to style HTML.
Biochemical process of fermentation of sucrose
The chemical equations below summarize the fermentation of sucrose (C12H22O11) into ethanol (C2H5OH). Alcoholic fermentation converts one mole of glucose into two moles of ethanol and two moles of carbon dioxide, producing two moles of ATP in the process.
The overall chemical formula for alcoholic fermentation is:
- C6H12O6 → 2 C2H5OH + 2 CO2
- C12H22O11 + H2O + invertase → 2 C6H12O6
- C6H12O6 + 2 ADP + 2 Pi + 2 NAD+ → 2 CH3COCOO− + 2 ATP + 2 NADH + 2 H2O + 2 H+
The chemical formula of pyruvate is CH3COCOO−. Pi stands for the inorganic phosphate.
The enzyme in step 3 is pyruvate decarboxylase.
Finally, pyruvate is converted to ethanol and CO2 in two steps, regenerating oxidized NAD+ needed for glycolysis:
- 1. CH3COCOO− + H+ → CH3CHO + CO2
catalyzed by pyruvate decarboxylase
- 2. CH3CHO + NADH+H+ → C2H5OH + NAD+
As shown by the reaction equation, glycolysis causes the reduction of two molecules of NAD+ to NADH. Two ADP molecules are also converted to two ATP and two water molecules via substrate-level phosphorylation.
Fermentation of sugar to ethanol and CO2 can also be done by Zymomonas mobilis, however the path is slightly different since formation of pyruvate does not happen by glycolysis but instead by the Entner–Doudoroff pathway. Other microorganisms can produce ethanol from sugars by fermentation but often only as a side product. Examples are
- Heterolactic acid fermentation in which Leuconostoc bacterias produce Lactate + Ethanol + CO2
- Mixed acid fermentation where Escherichia produce Ethanol mixed with Lactate, Acetate, Succinate, Formate, CO2 and H2
- 2,3-butanediol fermentation by Enterobacter producing Ethanol, Butanediol, Lactate, Formate, CO2 and H2
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The 4-subunit succinate:ubiquinone oxidorectase (EC 184.108.40.206) was first isolated by Hatefi and co-workers in 1962 and named "Complex II" to differentiate it from the other three respiratory complexes described in that paper. Unrelated reference .
- "What are TeX, LaTeX and friends?".
- Alexia Gaudeul (March 27, 2006). "Do Open Source Developers Respond to Competition?: The (La)TeX Case Study". SSRN .
- Leslie Lamport (April 23, 2007). "The Writings of Leslie Lamport: LaTeX: A Document Preparation System". Leslie Lamport's Home Page. Retrieved 2007-04-27.
- Stryer, Lubert (1975). Biochemistry. W. H. Freeman and Company. ISBN 0-7167-0174-X.
- Raj SB, Ramaswamy S, Plapp BV. "Yeast alcohol dehydrogenase structure and catalysis". Biochemistry. 53: 5791-803. doi:10.1021/bi5006442. PMID 25157460.
- Kagawa Y, Racker E. (1966). "Partial resolution of the enzymes catalyzing oxidative phosphorylation. 8. Properties of a factor conferring oligomycin sensitivity on mitochondrial adenosine triphosphatase". Journal of Biological Chemistry. 241: 2461–2466.
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|pmid=value (help). Check date values in:
- "this is the title". 1951. PMID 4223640.
- "this is the title". PMID 4223640.
- Venable, W. H.; Eckerle, K. L. "Didymium Glass Filters for Calibrating the Wavelength Scale of Spectrophotometers SRMs 2009, 2010, 2013 and 2014".
- BERNATH P, KEARNEY EB, SINGER TP. (1956). "Studies on succinic dehydrogenase. II. Isolation and properties of the dehydrogenase from beef heart". J Biol Chem. 223: 599–613. PMID 13385208.
- WANG TY, TSOU CL, WANG YL (1958). "Studies on succinic dehydrogenase. II. Further observations on the properties of the enzyme and its prosthetic group". Sci Sin. 7: 65–74. PMID 13529046.
- Y. Hatefi, A. G. Haavik, L. R. Fowler, and D. E. Griffiths (1962). "Studies on the Electron Transfer System: XLII. RECONSTITUTION OF THE ELECTRON TRANSFER SYSTEM". J. Biol. Chem. 1962 237:. 237: 2661–9. PMID 13905326.
- Thierry Ferreira, A. Brett Mason and Carolyn W. Slayman (2001). "The Yeast Pma1 Proton Pump: a Model for Understanding the Biogenesis of Plasma Membrane Proteins". J Biol Chem. 276: 29613–29616. doi:10.1074/jbc.R100022200.