Increase of Enzyme Activities following the in vitro Peroxidation of Normal Human Red Blood Cells

Enzyme ◽  
1988 ◽  
Vol 39 (1) ◽  
pp. 1-7 ◽  
Author(s):  
J. L. Vives Carrons ◽  
M. A. Pujades ◽  
D. Colomer
Author(s):  
Mustafa S. Al Musawi ◽  
M.S. Jaafar ◽  
B.T. Al-Gailani ◽  
Naser M. Ahmed ◽  
Fatanah M. Suhaimi

1971 ◽  
Vol 118 (545) ◽  
pp. 465-466 ◽  
Author(s):  
Ngo Tran ◽  
Marcel Laplante ◽  
Etienne Lebel

The decarboxylation of 3, 4-dihydroxyphenyl-alanine (Dopa) to dopamine has been shown previously in animal and human tissues in both in vitro and in vivo studies (Sourkes, 1966; Vogel et al., 1970). However, very little information is available as to whether or not the decarboxylation of Dopa occurs in human red blood cells (RBC). In the present experiment we demonstrated this change in RBC from normals and from schizophrenics. An ionization chamber method was used for an instantaneous and continuous measurement of 14CO2 production from DL-dopa-carboxyl-14C by RBC in vitro.


2019 ◽  
Vol 17 (1) ◽  
pp. 493-502 ◽  
Author(s):  
Maryam Faraji ◽  
Zahra Pourpak ◽  
Kazem Naddafi ◽  
Ramin Nabizadeh Nodehi ◽  
Mohammad Hossein Nicknam ◽  
...  

2019 ◽  
Vol 11 (3) ◽  
pp. 237-243 ◽  
Author(s):  
Montree Tungjai ◽  
Jetchada Sopapang ◽  
Natdanai Tasri ◽  
Chanatip Osothsongkroh ◽  
Attapon Jantarato ◽  
...  

1976 ◽  
Vol 128 (2) ◽  
pp. 184-187 ◽  
Author(s):  
Helen L. White ◽  
Malcolm N. McLeod ◽  
Jonathan R. T. Davidson

SummaryCatechol O-methyltransferase of lysed human red blood cells was assayed under optimal conditions, using saturating concentrations of the substrates, S-adenosyl-L-methionine and 3,4-dihydroxybenzoic acid. The mean enzyme activity found in 24 normal subjects was 29.2 nmol/hr/ml RBC. The mean activity in blood of 33 female unipolar depressives was not significantly different from normal. However, higher enzyme activities were observed in the blood of 11 schizophrenic patients (38.9 nmol/hr/ml RBC). Partially purified enzyme preparations from blood of normal and schizophrenic individuals were indistinguishable with respect to substrate specificities, isoelectric pH values, and ratios of the two O-methylated products. Therefore it is unlikely that any defect in O-methylation which may occur in schizophrenia can be attributed to a change in the intrinsic properties of erythrocyte catechol O-methyltransferase.


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