sulfur and enzymes/ Valentina

[Guest guest]

Hi, I don't quite follow you. First, only some enzymes have the

sulfhydrl groups. So these would be the ones getting deactivated by

the metals. Why would extra sulfur be a problem? I would think that

is you have extra sulfur that would help bing the metals and the

enzymes would not have so much competition and would therefore work

better. Also, isn't there a major effort to always try to get more

sulfur in AS people because of the low levels of natural sulfur? I

may be confusing two different things. Why is high sulfur bad?

I just found out that ALA contains sulfur. So is this one reason it

is such a fabulous chelator, because of the sulfhydryl groups?

.

[Guest guest]

Hi ,

First, thank you very much for the advice about the magnesium sulfate

on the A-M list. I really appreciate it, it will be very helpful. I

will probably come back to ask you a few questions if something will

not work well Thanks again.

About the sulfur and enzymes subject... It's really complicated. Well,

it sounds like this for me anyway, and I hope I won't say something

wrong. Where is Moria now to help me here? )

Anyway, I will try to tell you what I understood about sulfur and why

is not always good while chelation or in general for people who are

mercury toxic.

No, I will better " give " you what Andy Cutler says about this. It will

be way more accurate than I could explain it.

-------

The " sulfur " group in these foods is usually a thiol - an SH group

stuck onto the carbon backbone of a molecule somewhere. One of these

molecules is the amino acid cysteine. Many proteins in your body have

cysteine in them. Thus, your body is full of -SH groups that belong

to you.

If you take something that has one sulfur in it, then that just goes

and bumps the mercury off of one of the sulfurs that belong to you.

Next time that mercury runs into another sulfur that belongs to you it

might stick there. Since chlorella is just a good cysteine source,

and all the other " sulfur foods " contribute molecules that have one

sulfur in them in the active form, what happens is you make the

mercury atoms play pinball among the proteins in your body. They

bounce hither and yon - and mercury does its damage when it sticks to

a new sulfur group that belongs to you, or comes off of one. Since

the " sulfur foods " contribute molecules with one sulfur they don't

hold onto the mercury any better than you do, and they greatly

increase the amount of damage the mercury does without really removing

much of it.

Lipoic acid (as dihydrolipoate which your body converts it into),

DMSA and DMPS each have TWO thiols per molecule so they hold onto the

mercury atoms tighter than your body does and have a chance to really

escort the mercury out instead of just stirring it up. Thus these are

CHELATING AGENTS - chemicals with 2 or more binding groups per

molecule so they hold on to the metal atom tightly. Chlorella,

cysteine, penicillamine, glutathione, " sulfur foods, " etc. are not

chelating agents in any legitimate chemical sense.

---------

So this should tell you why sulfur or cysteine are not always good as

chelators or while you chelate or when you are heavy metal toxic. It's

about redistribution mainly. Sure, it's good for people low in sulfur

because it helps them make more sulfate and glutathion, which are

necessary for the body, but only when there is not a sulfur oxidation

problem. Sometimes, there are people low in sulfur but who cannot

" eat " cysteine or sulfur foods, because their body cannot metabolize

it (I suspect it's my son's case). This is why Epsom salt is so good

for these kids, because they cannot actually make their own sulfate.

As I said, people should check for plasma cysteine. This should give

a better idea.

High sulfur is not bad. At least I don't think it is. Bad is when you

have enough and eat more when you are trying to chelate.

Valentina

> Hi, I don't quite follow you. First, only some enzymes have the

> sulfhydrl groups. So these would be the ones getting deactivated by

> the metals. Why would extra sulfur be a problem? I would think that

> is you have extra sulfur that would help bing the metals and the

> enzymes would not have so much competition and would therefore work

> better. Also, isn't there a major effort to always try to get more

> sulfur in AS people because of the low levels of natural sulfur? I

> may be confusing two different things. Why is high sulfur bad?

>

> I just found out that ALA contains sulfur. So is this one reason it

> is such a fabulous chelator, because of the sulfhydryl groups?

> .

[Guest guest]

--- In @y..., " jornmatt " <kjorn@t...> wrote, in part:

> Why would extra sulfur be a problem? I would think that

> is you have extra sulfur that would help bing the metals and the

> enzymes would not have so much competition and would therefore work

> better. Also, isn't there a major effort to always try to get more

> sulfur in AS people because of the low levels of natural sulfur? I

> may be confusing two different things. Why is high sulfur bad?

>

> I just found out that ALA contains sulfur. So is this one reason it

> is such a fabulous chelator, because of the sulfhydryl groups?

> .

Hi , Okay, I went and found one of Andy's " more technical "

posts on this subject. I am quoting from:

/message/402

The text below is not the whole post, it is the part that

looked relevant to your question, to me. This was written

by Andy, and includes quotes of someone else who he is

responding to:

(sorry about the yucky formatting)

==============================================================

<< Andy and all,

Why should chlorella never be used as a chelator?

Also, why should

high sulfur foods not be used? >>

The " sulfur " group in these foods is usually a thiol -

an SH group stuck onto

the carbon backbone of a molecule somewhere. One of

these molecules is the

amino acid cysteine. Many proteins in your body have

cysteine in them.

Thus, your body is full of -SH groups that belong to

you.

If you take something that has one sulfur in it, then

that just goes and

bumps the mercury off of one of the sulfurs that

belong to you. Next time

that mercury runs into another sulfur that belongs to

you it might stick

there. Since chlorella is just a good cysteine source,

and all the other

" sulfur foods " contribute molecules that have one

sulfur in them in the

active form, what happens is you make the mercury

atoms play pinball among

the proteins in your body. They bounce hither and yon

- and mercury does its

damage when it sticks to a new sulfur group that

belongs to you, or comes

off of one. Since the " sulfur foods " contribute

molecules with one sulfur

they don't hold onto the mercury any better than you

do, and they greatly

increase the amount of damage the mercury does without

really removing much

of it.

Lipoic acid (as dihydrolipoate which your body

converts it into), DMSA and

DMPS each have TWO thiols per molecule so they hold

onto the mercury atoms

tighter than your body does and have a chance to

really escort the mercury

out instead of just stirring it up. Thus these are

CHELATING AGENTS -

chemicals with 2 or more binding groups per molecule

so they hold on to the

metal atom tightly. Chlorella, cysteine,

penicillamine, glutathione,

" sulfur foods, " etc. are not chelating agents in any

legitimate chemical

sense.