CHARACTERIZATION OF RAT LIVER AND KIDNEY ESTERASES

1967 ◽  
Vol 45 (4) ◽  
pp. 451-455 ◽  
Author(s):  
W. S. Schwark ◽  
D. J. Ecobichon

Vertical zone electrophoresis in starch gel was employed in conjunction with various histochemical techniques to characterize the liver and kidney esterases of male and female rats. Tissue-specific patterns were observed for each organ and a sex-dependent difference was noted on electrophoretic separation of the liver extracts. On the basis of substrate specificity and inhibitor sensitivity, both organs were observed to contain similar nonspecific aliesterases or carboxylesterases (EC 3.1.1.1). Inhibition studies showed the presence of two types of aliesterase in the liver and kidney extracts.

2012 ◽  
Vol 63 (4) ◽  
pp. 417-427 ◽  
Author(s):  
Mariana Tozlovanu ◽  
Delphine Canadas ◽  
Annie Pfohl-Leszkowicz ◽  
Christine Frenette ◽  
Robert J. Paugh ◽  
...  

AbstractIn the present study the photoreactivity of the fungal carcinogen ochratoxin A (OTA) has been utilised to generate authentic samples of reduced glutathione (GSH) and N-acetylcysteine (NAC) conjugates of the parent toxin. These conjugates, along with the nontoxic OTα, which is generated through hydrolysis of the amide bond of OTA by carboxypeptidase A, were utilised as biomarkers to study the metabolism of OTA in the liver and kidney of male and female Dark Agouti rats. Male rats are more susceptible than female rats to OTA carcinogenesis with the kidney being the target organ. Our studies show that the distribution of OTA in male and female rat kidney is not significantly different. However, the extent of OTA metabolism was greater in male than female rats. Much higher levels of OTα were detected in the liver compared to the kidney, and formation of OTα is a detoxification pathway for OTA. These findings suggest that differences in metabolism between male and female rats could provide an explanation for the higher sensitivity of male rats to OTA toxicity


1966 ◽  
Vol 44 (9) ◽  
pp. 1277-1283 ◽  
Author(s):  
D. J. Ecobichon

Proteins in aqueous extracts of breast muscle, leg muscle, cardiac muscle, liver, kidney, and spleen of adult cockerels were compared by zone electrophoresis in starch gel in sodium cacodylate or sodium citrate – phosphate systems. The proteins and enzymes were located in the starch gel by a variety of histochemical techniques. A partial characterization of the tissue esterases was carried out with various substrates and specific inhibitors. The 18 bands of esterases detected in tissues were aliesterases of two different types. Tissue specific enzymic patterns were obtained for esterases, alkaline phosphatase, acid phosphatase, lactate dehydrogenase, malate dehydrogenase, and isocitrate dehydrogenase. Glutamate dehydrogenase and glucose-6-phosphate dehydrogenase activity were detected only in the liver and kidney.


1966 ◽  
Vol 44 (6) ◽  
pp. 809-817 ◽  
Author(s):  
Sheila I. Read ◽  
E. J. Middleton ◽  
W. P. Mckinley

Female rats were fed diets low in minerals, vitamins, or protein, or a control diet, both alone and supplemented with 10 parts per million (p.p.m.) parathion for 3 weeks. Male and female rats were fed control and tow-vitamin diets both with and without parathion supplementation (0–10 p.p.m.) for 3 weeks. The liver and kidney carboxylesterases (EC 3.1.1.1.), and the plasma acetylcholinesterases (EC 3.1.1.7.) of the male rats, were measured.In the female rats, a low-mineral diet resulted in an increase of carboxylesterases in the liver and kidney; a low-vitamin diet caused a marked increase in liver carboxylesterases but had no effect on the carboxylesterases of the kidney. Parathion at 10 p.p.m. in all diets greatly reduced the liver carboxylesterases but had less effect on kidney carboxylesterases, except in the case of the low-protein diet, for which the reduction was similar to that in the liver. Varying amounts of parathion added to the low-vitamin diet reduced the liver and kidney carboxylesterases, but to a less extent than when added to the control diet.The liver carboxylesterases of male rats were inhibited approximately 50% by 2 p.p.m. parathion in the control diet and by 4 p.p.m. parathion in the low-vitamin diet. However, inhibition of plasma acetylcholinesterase and kidney carboxylesterases was not marked until the 10 p.p.m. parathion level was fed. The acetylcholinesterase activity of the plasma of male rats did not decrease until the level of liver carboxylesterases was very low.


1959 ◽  
Vol 197 (1) ◽  
pp. 135-137 ◽  
Author(s):  
Werner G. Heim

The relative concentrations of the various blood serum proteins, and especially of albumin, were found to be significantly different in male and female rats when examined by moving boundary or zone electrophoresis. However, no significant differences were noted in the sera obtained from rats at different points in the estrus cycle.


2021 ◽  
pp. 108786
Author(s):  
Sabino Valentina ◽  
Angelo Blasio ◽  
Antonio Ferragud ◽  
Sema G. Quadir ◽  
Malliga R. Iyer ◽  
...  

1980 ◽  
Vol 186 (1) ◽  
pp. 295-300 ◽  
Author(s):  
S Thrower ◽  
L Lim

The progestin-high-affinity-binding components in rat target tissues have been assayed by a simple and precise procedure by using spheroidal hydroxylapatite. The progestin ‘receptors’ in the uterus and hypothalamus of female rats are highly specific for progestins, which they bind with high affinity (Kd for [3H]progesterone in hypothalamus is 1.9 nM and in uterus is 3.7 nM). The dissociation of [3H]progesterone from receptor in vitro is rapid: t1/2 6 degrees C = 45 min in uterine cytosol; t1/2 6 degrees C = 160 min in hypothalamic cytosol. The binding is destroyed by proteinase. In the cytosol of hypothalamus and cortex of developing rats, progestin ‘receptors’ were present in both male and female rats by 2-3 days after birth; subsequent changes in concentration of these ‘receptors’ appeared to be independent of sex. Concentrations of progestin ‘receptor’ were close to adult values by 8-9 days, and thereafter changed relatively little.


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