P50 (pressure): Difference between revisions
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In [[biochemistry]], '''P50''' indicates the [[partial pressure]] of a [[gas]] required to achieve 50% [[enzyme]] saturation. Values of P50 are negatively correlated with substrate affinity, with lower values of P50 corresponding to high affinity and ''vice versa''. The term is analogous to the [[Michaelis-Menten constant]] (K<sub>m</sub>), which identifies the [[concentration]] of substrate required for an enzyme to achieve 50% of its maximum [[enzyme reaction rate|reaction velocity]]. |
In [[biochemistry]], '''P50''' indicates the [[partial pressure]] of a [[gas]] required to achieve 50% [[enzyme]] saturation. Values of P50 are negatively correlated with substrate affinity, with lower values of P50 corresponding to high affinity and ''vice versa''. The term is analogous to the [[Michaelis-Menten constant]] (K<sub>m</sub>), which identifies the [[concentration]] of substrate required for an enzyme to achieve 50% of its maximum [[enzyme reaction rate|reaction velocity]]. |
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For example, the P50 of [[myoglobin]] for [[oxygen|O<sub>2</sub>]] is |
For example, the P50 of [[myoglobin]] for [[oxygen|O<sub>2</sub>]] is 130 [[pascal]]s while the P50 for [[hemoglobin|adult hemoglobin]] is 3.5 kPa. Thus, when O<sub>2</sub> partial pressure is low, hemoglobin-bound O<sub>2</sub> is more readily transferred to myoglobin. Myoglobin, found in high concentrations in [[muscle]] tissue, can then transfer the oxygen to [[muscle fiber]]s, where it will be used in the generation of energy to fuel muscle contraction. |
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Revision as of 02:11, 21 January 2005
In biochemistry, P50 indicates the partial pressure of a gas required to achieve 50% enzyme saturation. Values of P50 are negatively correlated with substrate affinity, with lower values of P50 corresponding to high affinity and vice versa. The term is analogous to the Michaelis-Menten constant (Km), which identifies the concentration of substrate required for an enzyme to achieve 50% of its maximum reaction velocity.
For example, the P50 of myoglobin for O2 is 130 pascals while the P50 for adult hemoglobin is 3.5 kPa. Thus, when O2 partial pressure is low, hemoglobin-bound O2 is more readily transferred to myoglobin. Myoglobin, found in high concentrations in muscle tissue, can then transfer the oxygen to muscle fibers, where it will be used in the generation of energy to fuel muscle contraction.
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