myoglobin

This forum made possible through the generous support of SDN members, donors, and sponsors. Thank you.

co2013

Full Member
10+ Year Member
Joined
Jun 4, 2012
Messages
28
Reaction score
1
Active skeletal muscles demand oxygen so the high temp, co2, and acidity gives hemoglobin less affinity for O2 making it available to tissues. So why is it that myoglobin, which is present in muscles, has a HIGHER affinity for oxygen? Wouldn't give up less oxygen to muscles?

Members don't see this ad.
 
To tie in some other concepts - for the same reason that 2,3-BPG is upregulated in O2 deprivation and fetal hemoglobin has a higher affinity than adult hemoglobin - to get the O2 to where it needs to be.

Myoglobin - higher affinity facilitates uptake of O2 by peripheral tissue from hemoglobin

Fetal hemoglobin - higher affinity facilitates uptake of of O2 by fetal blood from maternal blood

2,3-BPG - upregulation in O2 deprivation facilitates additional unloading in the periphery
 
Top