allosteric effect vs cooperativevity

Discussion in 'DAT Discussions' started by arpitpatel86, Jun 3, 2008.

  1. arpitpatel86

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    destroyer number 166 when O2 binds to hemoglobin, we see an increased affinity for O2 binidng in the tremaining subunits.....what is this called....I thought it was allosteric effect but thats wrong it is actually cooperativity.....


    can some1 explain the differnce?
     
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  3. userah

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    allosteric effect and cooperativity are sort of opposites. allosteric effect is when something else binds to the enzyme's allosteric site (something besides the protein's active site) and this either enhances enzyme's productivity or decreases it. In general terms, O2 effects on hemoglobin does count as an allosteric effect but specifically what the question is asking for is in terms of cooperativity which states that as subunit attaches, it increases chances of another molecule of O2 attaching.I think in broad terms it's allosteric and more specifically it's cooperativity? hope someone else can back me up on this
     

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