A simple method to identify plasma amine oxidase activity band on polyacrylamide gel

1975 ◽  
Vol 69 (2) ◽  
pp. 637-642 ◽  
Author(s):  
Ada Wen-Shung Ma Lin ◽  
Donald O. Castell
Keyword(s):  
Oxidase Activity ◽  
Amine Oxidase ◽  
Polyacrylamide Gel ◽  
Simple Method ◽  
Plasma Amine Oxidase ◽  
Activity Band ◽  
Amine Oxidase Activity

Platelet and Plasma Amine Oxidase Activity in Alcoholic Individuals

1978 ◽  
Vol 132 (6) ◽  
pp. 548-554 ◽  
Author(s):  
Leslie F. Major ◽  
Dennis L. Murphy
Keyword(s):  
Oxidase Activity ◽  
Amine Oxidase ◽  
Hospital Treatment ◽  
Control Group ◽  
Platelet Mao ◽  
Plasma Amine Oxidase ◽  
Mao Activity ◽  
Platelet Mao Activity ◽  
Military Control ◽  
Amine Oxidase Activity

SummaryPlatelet and plasma amine oxidase activity was determined in a group of 99 healthy male (active duty military) alcoholics referred for hospital treatment who had been abstinent from alcohol for 2–10 days, and compared with that of a control military group. Platelet MAO activity was slightly but significantly lower in the alcoholic group. Both groups were significantly lower in MAO activity compared to a group of 42 non-military controls. In the alcoholic group there was no correlation between platelet MAO and severity or chronicity of drinking, nor was there evidence of iron deficiency to account for the lowered MAO activity. When the alcoholic and military control groups were split at the median, the first degree relatives of both the ‘low’ MAO alcoholics and the ‘low’ MAO military controls had a higher incidence of alcoholism than did the relatives of both ‘high’ MAO subgroups. No personal or family history data of alcohol-related problems were available on the non-military control group.

Effects of drugs on human blood platelet and plasma amine oxidase activity in vitro and in vivo

1968 ◽  
Vol 17 (1) ◽  
pp. 109-119 ◽  
Author(s):  
Donald S. Robinson ◽  
Walter Lovenberg ◽  
Harry Keiser ◽  
Albert Sjoerdsma
Keyword(s):  
Human Blood ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Blood Platelet ◽  
Human Blood Platelet ◽  
Plasma Amine Oxidase ◽  
Amine Oxidase Activity

scholarly journals Studies on the active site of pig plasma amine oxidase

1989 ◽  
Vol 264 (3) ◽  
pp. 663-669 ◽  
Author(s):  
D Collison ◽  
P F Knowles ◽  
F E Mabbs ◽  
F X Rius ◽  
I Singh ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Active Site ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Spectral Characteristics ◽  
Pyrroloquinoline Quinone ◽  
Amine Oxidases ◽  
Assay Procedure ◽  
Plasma Amine Oxidase ◽  
Amine Oxidase Activity

Amine oxidase from pig plasma (PPAO) has two bound Cu2+ ions and at least one pyrroloquinoline quinone (PQQ) moiety as cofactors. It is shown that recovery of activity by copper-depleted PPAO is linear with respect to added Cu2+ ions. Recovery of e.s.r. and optical spectral characteristics of active-site copper parallel the recovery of catalytic activity. These results are consistent with both Cu2+ ions contributing to catalysis. Further e.s.r. studies indicate that the two copper sites in PPAO, unlike those in amine oxidases from other sources, are chemically distinct. These comparative studies establish that non-identity of the Cu2+ ions in PPAO is not a requirement for amine oxidase activity. It is shown through the use of a new assay procedure that there are two molecules of PQQ bound per molecule of protein in PPAO; only the more reactive of these PQQ moieties is required for activity.

Genetic analysis of plasma amine oxidase activity in schizophrenia

1985 ◽  
Vol 15 (2) ◽  
pp. 121-132 ◽  
Author(s):  
Miron Baron ◽  
Neil Risch ◽  
Morton Levitt ◽  
Rhoda Gruen
Keyword(s):  
Genetic Analysis ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Plasma Amine Oxidase ◽  
Amine Oxidase Activity

scholarly journals Inhibition of beef plasma amine oxidase activity by glycine

FEBS Letters ◽  
1978 ◽  
Vol 94 (1) ◽  
pp. 112-114 ◽  
Author(s):  
M.T. Costa ◽  
S. Sabatini ◽  
P. Turini ◽  
B. Mondovì
Keyword(s):  
Oxidase Activity ◽  
Amine Oxidase ◽  
Plasma Amine Oxidase ◽  
Amine Oxidase Activity

Platelet and plasma amine oxidase activity in 680 normals: Sex and age differences and stability over time

1976 ◽  
Vol 16 (3) ◽  
pp. 254-265 ◽  
Author(s):  
D.L. Murphy ◽  
C. Wright ◽  
M. Buchsbaum ◽  
A. Nichols ◽  
J.L. Costa ◽  
...  
Keyword(s):  
Age Differences ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Plasma Amine Oxidase ◽  
Sex And Age Differences ◽  
Over Time ◽  
Amine Oxidase Activity

Mitochondrial Oxidation of p-N, N-Dimethylamino-β-Phenethylamine (DAPA)

1975 ◽  
Vol 33 ◽  
pp. 458-459
Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman
Keyword(s):  
Guinea Pig ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Histochemical Demonstration ◽  
Guinea Pig Heart ◽  
Pig Kidney ◽  
Cytoplasmic Vacuoles ◽  
Liver And Kidney ◽  
Mitochondrial Oxidation ◽  
Amine Oxidase Activity

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.

Acrolein produced from polyamines as one of the uraemic toxins

2003 ◽  
Vol 31 (2) ◽  
pp. 371-374 ◽  
Author(s):  
K. Sakata ◽  
K. Kashiwagi ◽  
S. Sharmin ◽  
S. Ueda ◽  
K. Igarashi
Keyword(s):  
Renal Failure ◽  
Chronic Renal Failure ◽  
Oxidase Activity ◽  
Culture Medium ◽  
Cellular Proliferation ◽  
Amine Oxidase ◽  
Early Stage ◽  
Chronic Glomerulonephritis ◽  
Toxic Compound ◽  
Amine Oxidase Activity

It is well known that the addition of spermine or spermidine to culture medium containing ruminant serum inhibits cellular proliferation. This effect is caused by the products of oxidation of polyamines that are generated by serum amine oxidase. Among the products, we found that acrolein is a major toxic compound produced from spermine and spermidine by amine oxidase. We then analysed the level of polyamines (putrescine, spermidine and spermine) and amine oxidase activity in plasma of patients with chronic renal failure. It was found that the levels of putrescine and the amine oxidase activity were increased, whereas spermidine and spermine were decreased in plasma of patients with chronic renal failure. The levels of free and protein-conjugated acrolein were also increased in plasma of patients with chronic renal failure. An increase in putrescine, amine oxidase and acrolein in plasma was observed in all cases such as diabetic nephropathy, chronic glomerulonephritis and nephrosclerosis. These results suggest that acrolein is produced during the early stage of nephritis through kidney damage and also during uraemia through accumulation of polyamines in blood due to the decrease in their excretion into urine.

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