scholarly journals ENZYMATIC OXIDATION OF PYRIDOXAMINE PHOSPHATE TO PYRIDOXAL PHOSPHATE IN RABBIT LIVER

1958 ◽  
Vol 232 (2) ◽  
pp. 761-776
Author(s):  
Burton M. Pogell
1963 ◽  
Vol 10 (01) ◽  
pp. 071-080 ◽  
Author(s):  
L. B Jaques ◽  
C Mary Jaques

SummaryPreparations were made of rabbit liver globulin by the method of Jaques for heparinase and their effect on heparin studied. The results confirmed the observations of a progressive loss of anticoagulant activity with globulin in 0.9% saline, of a loss of metachromatic activity after phenol extraction and the reversal of the latter by alkali. The latter observations were due to the solubility in phenol of heparin on combination with protein. With suitable preparations, a decrease in anticoagulant activity without decrease in metachromatic activity was observed, i.e. conversion of heparin to uroheparin. Loss of heparin due to combination with protein and resulting precipitation, solubility in phenol, etc. followed a protein pH-dissociation curve. Loss of heparin anticoagulant activity due to heparinase was maximal at pH 5.4. No loss of heparin occurred at pH values more acid than 5 or more alkaline than 7.


1960 ◽  
Vol XXXIII (IV) ◽  
pp. 532-538 ◽  
Author(s):  
H. Breuer ◽  
Gerta Pangels
Keyword(s):  

ABSTRACT The metabolism of oestrone, oestradiol-17α and oestradiol-17β has been studied in rabbit liver slices. Oestradiol-17α and oestradiol-17β were isolated as metabolites of oestrone. When oestradiol-17α17α was incubated oestrone and oestradiol-17β were formed, whereas oestradiol-17β gave rise to oestradiol-17α and oestrone. Quantitative experiments showed that after incubation of oestrone 5–8 times as much oestradiol-17β was found as oestradiol-17α.


Xenobiotica ◽  
1996 ◽  
Vol 26 (1) ◽  
pp. 1035-1055 ◽  
Author(s):  
A. A. Acheampong ◽  
D-S. Chien ◽  
S. Lam ◽  
S. Vekich ◽  
A. Breau ◽  
...  

1988 ◽  
Vol 20 (11-12) ◽  
pp. 167-173 ◽  
Author(s):  
S. E. Strand ◽  
R. M. Seamons ◽  
M. D. Bjelland ◽  
H. D. Stensel

The kinetics of methane-oxidizing bioreactors for the degradation of toxic organics are modeled. Calculations of the fluxes of methane and toxic chlorinated hydrocarbons were made using a biofilm model. The model simulated the effects of competition by toxics and mediane on their enzymatic oxidation by the methane monooxygenase. Dual-competitive-substrate/diffusion kinetics were used to model biofilm co-metabolism, integrating equations of the following form:where S1 and S2 are the local concentrations of methane and toxic compound, respectively, and r and K are the maximum uptake rates and Monod coefficients, and x is the distance into the biofilm.


2012 ◽  
Vol 8 (3) ◽  
pp. 196-205
Author(s):  
Massimo F.L. Pomponi ◽  
Massimiliano Pomponi ◽  
Giovanni Gambassi

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