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  2. Dissociation constant - Wikipedia

    en.wikipedia.org/wiki/Dissociation_constant

    In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) 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.

  3. Molecular mass - Wikipedia

    en.wikipedia.org/wiki/Molecular_mass

    When the molecular weight is given with the unit Da, it is frequently as a weighted average similar to the molar mass but with different units. In molecular biology, the mass of macromolecules is referred to as their molecular weight and is expressed in kDa, although the numerical value is often approximate and representative of an average.

  4. Dalton (unit) - Wikipedia

    en.wikipedia.org/wiki/Dalton_(unit)

    The molecular masses of proteins, nucleic acids, and other large polymers are often expressed with the unit kilodalton (kDa) and megadalton (MDa). [4] Titin , one of the largest known proteins, has a molecular mass of between 3 and 3.7 megadaltons. [ 5 ]

  5. Molar mass distribution - Wikipedia

    en.wikipedia.org/wiki/Molar_mass_distribution

    The mass average molar mass is calculated by ¯ = where N i is the number of molecules of molecular mass M i. The mass average molecular mass can be determined by static light scattering , small angle neutron scattering , X-ray scattering , and sedimentation velocity .

  6. Molecular weight cut-off - Wikipedia

    en.wikipedia.org/wiki/Molecular_weight_cut-off

    In ultrafiltration, the molecular weight cut-off or MWCO of a membrane refers to the lowest molecular weight of the solute (in daltons) for which 90% of the solute is retained by (prevented from passing through) the membrane, [1] or the molecular weight of the molecule (e.g. globular protein) that is 90% retained by the membrane.

  7. SDS-PAGE - Wikipedia

    en.wikipedia.org/wiki/SDS-PAGE

    Proteins of the erythrocyte membrane separated by SDS-PAGE according to their molecular masses. SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) is a discontinuous electrophoretic system developed by Ulrich K. Laemmli which is commonly used as a method to separate proteins with molecular masses between 5 and 250 kDa.

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    mail.aol.com

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  9. Urease - Wikipedia

    en.wikipedia.org/wiki/Urease

    The molecular weight is either 480 kDa or 545 kDa for jack-bean urease (calculated mass from the amino acid sequence). 840 amino acids per molecule, of which 90 are cysteine residues. [9] The optimum pH is 7.4 and optimum temperature is 60 °C. Substrates include urea and hydroxyurea.