Effects of Heparin on Lipolytic Enzyme Activities in vivo and in vitro

Enzyme ◽  
1976 ◽  
Vol 21 (1) ◽  
pp. 21-29 ◽  
Author(s):  
J. Patelski ◽  
Z. Waligora ◽  
A.N. Howard
1980 ◽  
Vol 30 (1) ◽  
pp. 65-73 ◽  
Author(s):  
Takako TOMITA ◽  
Ikumi YONEKURA ◽  
Yasufumi SHIRASAKI ◽  
Eiichi HAYASHI ◽  
Fujio NUMANO

2011 ◽  
Vol 1 (1) ◽  
pp. 4 ◽  
Author(s):  
Hansen W. Murcia ◽  
Gonzalo J. Díaz ◽  
Sandra Milena Cepeda

Cytochrome P450 enzymes (CYP) are a group of monooxygenases able to biotransform several kinds of xenobiotics including aflatoxin B1 (AFB1), a highly toxic mycotoxin. These enzymes have been widely studied in humans and others mammals, but there is not enough information in commercial poultry species about their biochemical characteristics or substrate specificity. The aim of the present study was to identify CYPs from avian liver microsomes with the use of prototype substrates specific for human CYP enzymes and AFB1. Biochemical characterization was carried out in vitro and biotransformation products were detected by high-performance liquid chromatography (HPLC). Enzymatic constants were calculated and comparisons between turkey, duck, quail and chicken activities were done. The results demonstrate the presence of four avian ortholog enzyme activities possibly related with a CYP1A1, CYP1A2, CYP2A6 (activity not previously identified) and CYP3A4 poultry orthologs, respectively. Large differences in enzyme kinetics specific for prototype substrates were found among the poultry species studied. Turkey liver microsomes had the highest affinity and catalytic rate for AFB1 whereas chicken enzymes had the lowest affinity and catalytic rate for the same substrate. Quail and duck microsomes showed intermediate values. These results correlate well with the known in vivo sensitivity for AFB1 except for the duck. A high correlation coefficient between 7-ethoxyresorufin-Odeethylase (EROD) and 7-methoxyresorufin- O-deethylase (MROD) activities was found in the four poultry species, suggesting that these two enzymatic activities might be carried out by the same enzyme. The results of the present study indicate that four prototype enzyme activities are present in poultry liver microsomes, possibly related with the presence of three CYP avian orthologs. More studies are needed in order to further characterize these enzymes.


1972 ◽  
Vol 50 (4) ◽  
pp. 767-786 ◽  
Author(s):  
R. A. A. Morrall ◽  
L. J. Duczek ◽  
J. W. Sheard

One hundred and fourteen isolates of Sclerotinia from 23 different hosts in many parts of Saskatchewan were grouped, according to their morphology, on minimal medium. Two types of seedling pathogenicity tests on six host species were conducted on at least one isolate from each morphological group and one from each host species. A total of 38 isolates was tested. Assays for pectolytic enzyme activities of the same 38 isolates were done using a defined medium, and Swede turnip and carrot tissue as substrates. Polygalacturonase, pectin transeliminase, and pectin methylesterase were all tested. The results showed that an endopolygalacturonase was probably the most prevalent enzyme. Some isolates also produced exopolygalacturonase and pectin methylesterase, but pectin transeliminase was never detected. There was no correlation between pathogenicity of the isolates and their enzyme activities in vitro or in vivo, suggesting that pectolytic enzymes are not responsible alone for pathogenicity. Agglomerative classification was used to demonstrate relationships between the isolates. However, the isolates did not fall into discrete groups based on morphological, pathological, physiological, or even combined characteristics. Neither were there clear host or geographic associations. This continuous variation rather than a segregated population is consistent with Purdy's "broader concept of the species S. sclerotiorum."


2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Amol L. Shirfule ◽  
Venkatesh Racharla ◽  
S. S. Y. H. Qadri ◽  
Arjun L. Khandare

Gokshuradi Yog (GY)is a polyherbal ayurvedic formulation used traditionally for several decades in India for the treatment of urolithiasis. The aim of the present study was to determine the underlying mechanism ofGYaction in the management of calcium oxalate urolithiasis. The effect ofGokshuradi polyherbal aqueous extracts(GPAEs) was studied on various biochemical parameters involved in calcium oxalate formation by employingin vitroandin vivomethods.GPAEexhibited significant antioxidant activity against 1, 1-diphenyl-2-picrylhydrazyl free radical and inhibited lipid peroxidation in thein vitroexperiments. The rat model of urolithiasis induced by 0.75% ethylene glycol (EG) and 1% ammonium chloride (AC) in water caused polyuria, weight loss, impairment of renal function, and oxidative stress and decreased antioxidant enzyme activities in untreated control groups. However,GPAE-(25, 50, and 100 mg/kg) treated groups caused diuresis accompanied by a saluretic effect and revealed significant increase in antioxidant enzyme activities along with decreased oxalate synthesizing biochemical parameters at higher doses. This study revealed the antiurolithic effect ofGPAEmediated possibly through inhibiting biochemical parameters involved in calcium oxalate formation, along with its diuretic and antioxidant effects, hence supporting its use in the treatment of calcium oxalate urolithiasis.


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