Rat brain aryl acylamidase: Multiple forms and inhibition effects of LSD, serotonin and related compounds

Louise L. Hsu; Steven M. Paul; Angelos E. Halaris; Daniel X. Freedman

doi:10.1016/0024-3205(77)90038-8

Rat brain aryl acylamidase: Multiple forms and inhibition effects of LSD, serotonin and related compounds

Louise L. Hsu, Steven M. Paul, Angelos E. Halaris, Daniel X. Freedman

Washington University School of Medicine

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

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Abstract

At least two forms of aryl acylamidase (E.C.3.5.1.13, AAA) were separated from rat brain extracts by ammonium sulfate precipitation (33-60% saturation) and subsequent Bio-Gel column chromatography. Fraction AAA-1 showed pH optimum at 7.5 whereas AAA-2 showed a pH optimum at 5.5 AAA-1 activity was markedly inhibited at pH 7.5 by d-LSD and 2-Br-LSD, moderately inhibited by 5-HT and slightly inhibited by tryptamine but it was not affected by 1-LSD, at 0.1 mM concentration. AAA-2 was only moderately inhibited at pH 5.5 by d-LSD and 2-Br-LSD but not affected by 1-LSD, 5-HT or tryptamine at the same concentrations. Catecholamines and their structurally related drugs had no significant effects on either enzyme activity. Kinetic studies with AAA-1 indicated competitive inhibition by d-LSD with a K_i value of 4.90 ± 0.61 μM.

Original language	English
Pages (from-to)	857-865
Number of pages	9
Journal	Life Sciences
Volume	20
Issue number	5
DOIs	https://doi.org/10.1016/0024-3205(77)90038-8
State	Published - Mar 1 1977

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title = "Rat brain aryl acylamidase: Multiple forms and inhibition effects of LSD, serotonin and related compounds",

abstract = "At least two forms of aryl acylamidase (E.C.3.5.1.13, AAA) were separated from rat brain extracts by ammonium sulfate precipitation (33-60% saturation) and subsequent Bio-Gel column chromatography. Fraction AAA-1 showed pH optimum at 7.5 whereas AAA-2 showed a pH optimum at 5.5 AAA-1 activity was markedly inhibited at pH 7.5 by d-LSD and 2-Br-LSD, moderately inhibited by 5-HT and slightly inhibited by tryptamine but it was not affected by 1-LSD, at 0.1 mM concentration. AAA-2 was only moderately inhibited at pH 5.5 by d-LSD and 2-Br-LSD but not affected by 1-LSD, 5-HT or tryptamine at the same concentrations. Catecholamines and their structurally related drugs had no significant effects on either enzyme activity. Kinetic studies with AAA-1 indicated competitive inhibition by d-LSD with a Ki value of 4.90 ± 0.61 μM.",

author = "Hsu, {Louise L.} and Paul, {Steven M.} and Halaris, {Angelos E.} and Freedman, {Daniel X.}",

note = "Funding Information: This work was supported by USPFiS Research Grant Mr . Robert Chang for performing the assays .",

year = "1977",

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doi = "10.1016/0024-3205(77)90038-8",

language = "English",

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T1 - Rat brain aryl acylamidase

T2 - Multiple forms and inhibition effects of LSD, serotonin and related compounds

AU - Hsu, Louise L.

AU - Paul, Steven M.

AU - Halaris, Angelos E.

AU - Freedman, Daniel X.

N1 - Funding Information: This work was supported by USPFiS Research Grant Mr . Robert Chang for performing the assays .

PY - 1977/3/1

Y1 - 1977/3/1

N2 - At least two forms of aryl acylamidase (E.C.3.5.1.13, AAA) were separated from rat brain extracts by ammonium sulfate precipitation (33-60% saturation) and subsequent Bio-Gel column chromatography. Fraction AAA-1 showed pH optimum at 7.5 whereas AAA-2 showed a pH optimum at 5.5 AAA-1 activity was markedly inhibited at pH 7.5 by d-LSD and 2-Br-LSD, moderately inhibited by 5-HT and slightly inhibited by tryptamine but it was not affected by 1-LSD, at 0.1 mM concentration. AAA-2 was only moderately inhibited at pH 5.5 by d-LSD and 2-Br-LSD but not affected by 1-LSD, 5-HT or tryptamine at the same concentrations. Catecholamines and their structurally related drugs had no significant effects on either enzyme activity. Kinetic studies with AAA-1 indicated competitive inhibition by d-LSD with a Ki value of 4.90 ± 0.61 μM.

AB - At least two forms of aryl acylamidase (E.C.3.5.1.13, AAA) were separated from rat brain extracts by ammonium sulfate precipitation (33-60% saturation) and subsequent Bio-Gel column chromatography. Fraction AAA-1 showed pH optimum at 7.5 whereas AAA-2 showed a pH optimum at 5.5 AAA-1 activity was markedly inhibited at pH 7.5 by d-LSD and 2-Br-LSD, moderately inhibited by 5-HT and slightly inhibited by tryptamine but it was not affected by 1-LSD, at 0.1 mM concentration. AAA-2 was only moderately inhibited at pH 5.5 by d-LSD and 2-Br-LSD but not affected by 1-LSD, 5-HT or tryptamine at the same concentrations. Catecholamines and their structurally related drugs had no significant effects on either enzyme activity. Kinetic studies with AAA-1 indicated competitive inhibition by d-LSD with a Ki value of 4.90 ± 0.61 μM.

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U2 - 10.1016/0024-3205(77)90038-8

DO - 10.1016/0024-3205(77)90038-8

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C2 - 15714771

AN - SCOPUS:0017576173

SN - 0024-3205

VL - 20

SP - 857

EP - 865

JO - Life Sciences

JF - Life Sciences

IS - 5

ER -

Rat brain aryl acylamidase: Multiple forms and inhibition effects of LSD, serotonin and related compounds

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