The Claim

The deiodination rate of T3 sulfate in human liver microsomes is approximately 30 times faster than the deiodination rate of unsulfated T3, indicating that sulfation enhances substrate recognition by deiodinase enzymes.

Source: Deiodination of thyroid hormone by human liver.

What the research says

Supports is higher

Support is ahead, but a single strong opposing study can change this.

Supports
20score
Challenges
0score

These are independent scores, not a percentage. Higher-grade studies count more, so a single strong opposing study can outweigh several weaker ones.

How it works
1 study reviewed
In plain English

In human liver tissue, T3 sulfate is converted by deiodinase enzymes about 30 times faster than unsulfated T3, showing that the addition of a sulfate group increases the enzyme's efficiency in processing this hormone.

See the scientific wording

The deiodination of T3 sulfate occurs approximately 30 times faster than that of unsulfated T3 in human liver microsomes, indicating sulfation significantly enhances substrate recognition by the deiodinase enzyme.

Why this might work

Adding a sulfate group to the thyroid hormone makes it fit much better into the liver enzyme that removes iodine, so the enzyme can break it down 30 times faster than the unsulfated version.

Verified mechanismbased on 1 study

What the research says

1 study
  1. Study: Deiodination of thyroid hormone by human liver.

    Scientists found that when a sulfate group is added to a thyroid hormone, the liver breaks it down about 30 times faster than the normal version — meaning the sulfate tag makes it easier for the liver’s enzyme to recognize and remove it.

Score breakdown, mechanism chain, raw evidence, ideal studies needed & 1 supporting studies

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