Results 281 to 290 of about 112,050 (329)

Platelet monoamine oxidase-B activity in Parkinson's disease

Journal of Neural Transmission - Parkinson's Disease and Dementia Section, 1989
Platelet MAO-B levels have been investigated in seventeen consecutively diagnosed and previously untreated patients with idiopathic Parkinson's disease using the non-hydroxylated catecholamine, beta-phenylethylamine, as substrate. Patients with Parkinson's disease had MAO-B activity levels that were considerably higher than sex and age matched normal ...
G B, Steventon, S G, Sturman, M T, Heafield, R H, Waring, J, Napier, A C, Williams   +5 more
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Chromenylchalcones with inhibitory effects on monoamine oxidase B

Bioorganic & Medicinal Chemistry, 2013
Structure-activity relationship (SAR) calculations were used to find monoamine oxidase-B (MAO-B) inhibitors by identifying pharmacophores exhibiting high inhibitory activities. Several such chromenylchalcones were designed and synthesized accordingly. Their inhibitory effects on MAO-B were determined using an HPLC-based method and an MAO-B enzyme assay
Geunhyeong, Jo, Seunghyun, Ahn, Bong-Gyu, Kim, Hye Ri, Park, Young Hwa, Kim, Hyun Ah, Choo, Dongsoo, Koh, Youhoon, Chong, Joong-Hoon, Ahn, Yoongho, Lim   +9 more
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Direct Continuous Fluorometric Assay for Monoamine Oxidase B

Analytical Biochemistry, 1996
The first direct and continuous fluorometric assay for monoamine oxidase B (MAO B) has been developed. E-2,5-Dimethoxycinnamylamine hydrochloride was designed and synthesized and was found to be an excellent substrate for MAO B (Km = 218 microM, Kcat = 435 min-1).
J J, Zhou, B, Zhong, R B, Silverman
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Molecular properties of monoamine oxidases A and B

Psychopharmacology, 1992
Monoamine oxidases A and B (MAO-A and B) catalyze the oxidative catabolism of biogenic amines and xenobiotics. Investigation of these mitochondrial membrane proteins shows that they differ in substrate preference, inhibitor specificity, tissue and neuronal cell distribution, immunological properties, and nucleotide and deduced amino acid sequences ...
S W, Kwan, J M, Bergeron, C W, Abell
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MONOAMINE OXIDASE A AND B IN CULTURED CELLS

Journal of Neurochemistry, 1978
Abstract— Monoamine oxidase (MAO) activity against tryptamine was compared in a number of continuous rodent lines, including neuroblastoma, hepatoma, melanoma, nephroma, sarcoma and L cells. Activities against tryptamine varied over 300‐fold in homogenates of different lines, being highest in hepatoma line MH1C1 and lowest in a neuroblastoma line ...
M, Hawkins, X O, Breakefield
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Monoamine oxidase A and B: A useful concept?

Biochemical Pharmacology, 1978
The use of a number of inhibitors of monoamine oxidasc (monoamine:O, oxidoreductase, EC 1.4.3.4) has shown that many mam~lian tissues contain two major forms of the enzymic activity that differ in their substrate specificities and sensitivities to inhibitors.
Christopher J. Fowler, Brian A. Callingham, Timothy J. Mantle, Keith F. Tipton   +3 more
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Localization of distinct monoamine oxidase a and monoamine oxidase b cell populations in human brainstem

Neuroscience, 1988
Monoclonal antibodies, specific for either monoamine oxidases A or B, were used to determine the localization of monoamine oxidase in the human brain. Two distinct populations of neurons were detected by immunocytochemical staining. Neurons in regions rich in catecholamines were positive for monoamine oxidase A, including the nucleus locus coeruleus ...
K N, Westlund, R M, Denney, R M, Rose, C W, Abell   +3 more
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Molecular characterization of monoamine oxidases A and B

2000
Monoamine oxidase A and B (MAO A and B) are the major neurotransmitter-degrading enzymes in the central nervous system and in peripheral tissues. MAO A and B cDNAs from human, rat, and bovine species have been cloned and their deduced amino acid sequences compared.
C W, Abell, S W, Kwan
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Monoamine Oxidase B Inhibitors

CNS Drugs, 1996
Danièle Bentué-Ferrer, Gaëlle Ménard, Hervé Allain   +2 more
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Monoamine Oxidase B Activity in Senile Plaque

1990
Two types of monoamine oxidase (MAO; EC 1.4.3.4), MAO-A and MAO-B, has been demonstrated on the basis of their inhibitor specificities and substrate preferences (Johnston, 1968; Knoll and Magyar, 1972; Glover et al., 1977; Fowler et al., 1980; Garrick and Murphy, 1980).
Shinichi Nakamura, Osamu Yasuhara, Toshio Kawamata, Toru Kimura, Ichiro Akiguchi, Jun Kimura, Masakuni Kameyama, Noriko Nakamura, Hiroshi Kimura   +8 more
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