• Welcome to the DeeperBlue.com Forums, the largest online community dedicated to Freediving, Scuba Diving and Spearfishing. To gain full access to the DeeperBlue.com Forums you must register for a free account. As a registered member you will be able to:

    • Join over 44,280+ fellow diving enthusiasts from around the world on this forum
    • Participate in and browse from over 516,210+ posts.
    • Communicate privately with other divers from around the world.
    • Post your own photos or view from 7,441+ user submitted images.
    • All this and much more...

    You can gain access to all this absolutely free when you register for an account, so sign up today!

myoglobin levels

Thread Status: Hello , There was no answer in this thread for more than 60 days.
It can take a long time to get an up-to-date response or contact with relevant users.
"On the other hand, I have yet to see a photo of a hulking, muscle-bound, elite freediver. What's up with that!?!?!"

Doesn't Pipin go 6' 2" at 210lbs? Thats pretty bulky...
To add to what Eric said - and to answer the question about whether Myoglobin could ver release O2 to the blood:

Never - because the dissociation curves of ppO2 for Myo- and Haemoglobin never cross each other. Human myoglobin will steal O2 from haemoglobin everytime irrelevant of the ppO2.

Which is shame - because it would help us as Freedivers if it weren't the case. The best we can do is reduce blood flow to muscles so that desaturated myoglobin does not get the chance to replenish O2 from the blood.

Actually, since both the hemoglobin-O2 and myoglobin-O2 dissociation curves are functions of temperature, pH, and possible 2,3-DPG, it is possible, under near-impossible circumstances, for O2 to travel from myoglobin to blood.

If, for example, the muscle were extremely acidic, both the blood and myoglobin (in the muscle) would be less sticky to oxygen, and then if some totally alkaline, cold blood suddenly flowed into the muscle, the myoglobin could theoretically, for a tiny instant, give up its O2... since the myoglobin would still be very acidic/warm (less affinity for O2), and the blood would be very alkaline/cold (high O2 affinity), although this condition would only persist for a fraction of a second, before the acidity & temperature equalize.

Eric Fattah
BC, Canada
My experiment ...

Ok, I am just about to inject cold baking soda into my veins. I'll get back to you all to let you know how I made out ... :blackeye
As soon as I think I understand something, you all contrive to confuse me again. Let's see if I can make the link to another thread...

Would another way to stop myglobin stealing O2 from the blood be to 'sprint' and therefore get the muscles working anaeobically?

Nice idea Eric - and how shall we plan to get acidic muscles with no blood flow that still have saturated myoglobin?:D

You do come up with some wacky ideas - :friday

It is really nice to see someone looking at these issues in such great depth.

Al - the idea of sprinting sadly doesn't work because the O2 is stolen from the myoglobin during anearobic metabolism because whereas the energy is produced anaerobically - the py products need to be metabolised immediately by the oxygen in the myoglobin.
hmmm - a tad toxic!

Another one is to eat some NaCO3. might supress the urge to breathe, but will vastly increase your likelihood of catching Cholera and many, many other diseases!

DeeperBlue.com - The Worlds Largest Community Dedicated To Freediving, Scuba Diving and Spearfishing


ISSN 1469-865X | Copyright © 1996 - 2024 deeperblue.net limited.

DeeperBlue.com is the World's Largest Community dedicated to Freediving, Scuba Diving, Ocean Advocacy and Diving Travel.

We've been dedicated to bringing you the freshest news, features and discussions from around the underwater world since 1996.