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1) "Konica" -- As to konica kd
Konica | | Fate | merged | | | Successor | Konica Minolta | | Founded | 1873 | | Defunct | August 5, 2003 | | Location | Japan |
Konica (コニカ, Konika?) was a Japanese manufacturer of, among other products, film, film cameras, camera accessories, photographic and photo-processing equipment, photocopiers, fax machines and laser printers. The company traced its history back to 1873 (pre-dating Kodak in the photography business) when pharmacist Rokusaburo Sugiura began selling photographic materials at his store.
On August 5, 2003, Konica merged with Minolta to form Konica Minolta. In March 2007 the new company will close down its photo imaging division, which produces color film, color paper, photo chemicals and digital minilab machines. Its digital SLR camera section has been transferred to Sony. Dai Nippon will purchase Konica's Odawara factory site and continue to produce paper under its own brand, while Seapac will acquire the Konica chemical factory. - 1 History
- 2 Products
- 2.1 Film
- 2.2 Cameras
- 2.2.1 35mm Rangefinder
- 2.2.2 F-mount SLRs
- 2.2.3 AR-mount SLRs
- 2.3 Lenses
- 3 See also
- 4 References
- 5 External links
| Konica was a major producer of 35mm film and related products, including film development processors and printing technology. Whil..."
2) "Kd" -- As to konica kd KD
Function: abbreviation
1 kiln-dried
2 knockdown; knocked down Pronunciation Symbols
In chemistry and biochemistry, a dissociation constant is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions. The dissociation constant is usually denoted Kd and is the inverse of the affinity constant. In the special case of salts, the dissociation constant can also be called an ionization constant. For a general reaction in which a complex AxBy breaks down into x A subunits and y B subunits, the dissociation constant is defined where [A], [B], and [AxBy] are the concentrations of A, B, and the complex AxBy, respectively. - 1 Protein-Ligand binding
- 2 Another notation
- 3 Dissociation constant of water
- 4 Acid base reactions
- 5 See also
| Dissociation constants are commonly used to describe how tightly a ligand (such as a drug) binds to a protein. Such binding is usually non-covalent, i.e., no chemical bonds are made or broken. Since the binding is usually described by a two-state process the corresponding dissociation constant is defined where [P], [L] and [C] represent the concentrations of the protein, ligand and bound complex, respectively. The dissociation constant has the units of molar (M), and corresponds to the concentration of ligand [L] at which the binding site on the protein is half occupied, i.e., when the concentration of protein with ligand bound [C] equals the concentration of protein with no ligand bound [P]. The smaller the dissociation constant, the more tightly bound the ligand is; for example, a ligand with a nanomolar (nM) dissociation constant binds more tightly than..."
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