scholarly journals Lipolytic Enzyme Activity in Lysosomal Fraction from Porcine Muscle and Liver

1984 ◽  
Vol 55 (1) ◽  
pp. 36-44
Author(s):  
Yukihiro TOMITA ◽  
Kiyomi NAGAYAMA ◽  
Fumio OHTAKA
1983 ◽  
Vol 54 (3) ◽  
pp. 209-212
Author(s):  
Yukihiro TOMITA ◽  
Kiyomi NAGAYAMA ◽  
Fumio OHTAKA

Plant Science ◽  
1988 ◽  
Vol 55 (3) ◽  
pp. 205-211 ◽  
Author(s):  
Robert A. Moreau ◽  
Charles P. Morgan

1987 ◽  
Vol 67 (2) ◽  
pp. 301-318 ◽  
Author(s):  
E. R. FARNWORTH ◽  
J. K. G. KRAMER

At birth, piglets have little body fat that can be mobilized. The influx of high-fat milk causes a rapid increase in body fat stores and a depression of lipogenic enzyme activity. Conversely, lipolytic enzyme activity increases after birth. Changing the fat intake of sucking piglets affects the amount of fat deposition. The length of the sucking period also influences body composition at weaning. Weaning produces a pronounced but temporary decrease in total body lipid, despite an increase in fat synthesis. The effect of weaning on lipolysis is not clear due to a lack of experimental data. During the growing period, fat continues to build up even though lipogenic enzyme activity tends to decline with age. The composition of the diet, the sex of the animal and genetic factors have all been shown to influence the rate of lipogenesis. Fewer reports have been published in which factors affecting lipolysis have been studied and the results are often less conclusive. However, the combined activities of lipogenic and lipolytic processes do not account for the large quantity of body fat found in growing pigs. Key words: Swine, fat, lipogenesis, lipolysis, diet, sex.


2011 ◽  
Vol 58 (112) ◽  
Author(s):  
Sophocles Lanitis ◽  
Evangelos Lolis ◽  
Nikolaos Dafnios ◽  
Constantine Karaliotas ◽  
Dionysios Voros ◽  
...  

Author(s):  
Ellen George ◽  
Candan Tamerler ◽  
Angel Martinez ◽  
Maria Jesus Martinez ◽  
Tajalli Keshavarz

1979 ◽  
Vol 27 (10) ◽  
pp. 1317-1321 ◽  
Author(s):  
N W Revis ◽  
J P Durham

Previous studies have described a decrease in the activity of adenylate cyclase in the parotid gland of isoproterenol-treated rats. In the present studies, a similar decrease was observed in mice treated with isoproterenol. Studies on the subcellular distribution of adenylate cyclase after isoproterenol stimulation of the parotid gland showed that enzyme activity was increased in the lysosomal fraction and decreased in the cellular membrane fractions. Cytochemical studies on the localization of adenylate cyclase in stimulated gland showed an increase in vesicles which contained enzyme activity and a decrease in activity at the luminal and plasma membranes. It is suggested, based on the present findings and results reported by other investigators, that after isoproterenol stimulation of the parotid gland, adenylate cyclase (along with excess membrane) is degraded by lysosomes. If this suggestion is true, then the observed decrease in adenylate cyclase would have a molecular explanation.


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