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Results and discussion Modified dDAT resembles hNET primary substrate-binding site The dDAT, much like its human counterparts hDAT and hNET, is capable of interacting with both DA ( K i = 2.0 M) and NE ( K i = 19.1 M) with varying efficacies (Fig

Lin W, Ye H

While more large-scale human studies are needed, current research and clinical use suggest that BPC-157 is well tolerated and low-risk when used under medical supervision

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Unlike many mammals, humans lack the enzyme uricase, which degrades UA to the more soluble compound allantoin

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