Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better.

TZ Jones; D Balsa; M Unzeta; RR. Ramsay

doi:10.1007/s00702-007-0675-y

Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better.

Translated title of the contribution: Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better.

TZ Jones, D Balsa, M Unzeta, RR. Ramsay

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

41 Citations (Scopus)

Translated title of the contribution	Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better.
Original language	Multiple languages
Pages (from-to)	707-712
Journal	Journal of Neural Transmission
Volume	114
Issue number	6
DOIs	https://doi.org/10.1007/s00702-007-0675-y
Publication status	Published - 1 Jan 2007

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10.1007/s00702-007-0675-y

Cite this

@article{3041f2fcae0d44f898f40e6e7b95615d,

title = "Variations in activity and inhibition with pH: the protonated amine is the substrate for monoamine oxidase, but uncharged inhibitors bind better.",

author = "TZ Jones and D Balsa and M Unzeta and RR. Ramsay",

year = "2007",

month = jan,

day = "1",

doi = "10.1007/s00702-007-0675-y",

language = "M{\'u}ltiples idiomas",

volume = "114",

pages = "707--712",

number = "6",

}