Behavior of enzymes in liver of starved rats

Allard, C.; Lamirande, Gaston de; Cantero, Antonio

doi:10.1016/0014-4827(57)90044-7

Cited by 43 publications

(13 citation statements)

References 20 publications

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“…This apparent increase disappears when the amount of total WNA and protein per total liver is considered. The observed loss of 40% is in agreement with the reported loss of 50% of the total RNA and protein (2).…”

Section: Discussiormsupporting

confidence: 93%

“…Allard et a/. (2) have shown that the total activities of the acid and alkaline ribssnucleases of rat liver decreased by 35 and 28%, respectively. This shows that the increased capacity of autodegradation of the starved animals is due to a diKerent RNase.…”

Section: Discussiormmentioning

confidence: 97%

“…In starved, adult rats, the number of cells per liver remains constant although the liver loses 50% sf its normal weight (1,2). RNA and protein contents per liver similarity decrease by 50% (2-4).…”

mentioning

confidence: 97%

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The Influence of Starvation on Rat Liver Polysomes

Arora¹,

Lamirande²

1971

Can. J. Biochem.

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AWORA, D. 9. S.. and DE I,AMIWANDE, G . The influence of starvation on rat liver polysomes. Can. J. Blschem. 49,1150Blschem. 49, -% 154 (1971.A $-day starvation produced a marked effect on the ribosomal profile of rat liver by decreasing heavier polysomes and increasing lighter ones. When starved rats were refed for 24 h, a rapid formation of heavier polysornes was detected with a concurrent decrease in the lighter polysomes. On comparing the autodegradation capacity of the hepatic ribosomes of starved, starved-refed, and contra1 animals, it was found that starved rats were about five times more active than starved-refed rats and 44% more active than the controls. ARORA, B. 9. S., et DE LAMIRANDE, G . The influence of starvation on rat liver polysomes. C&n. J. Biochem. 49, f 150-1 154 (1971).Un jeQne de six jours produit un eEet marque sur Ie profil ribosornique du foie de rat. Les polysomes plus lourds diminuent et les plus l6gers augmentent. Si apr&s le jeQne Ies rats ssnt nourris durant 24 heures, il y a formation rapide de polysomes plus lourds et diminution simultanee des polysomes plus lCgers. La cornpamison du pouvoir d9autodkgradation des ribosomes hkpatiques chez les animaux h jeun, chez les a n h a u x nourris aprts le jeane et chez les t&mohs, montre que le pouvoir des rats B jeun est 5 fois plus actif que celui dea rats raourris apr6s le jeBne et 44% plus actif que celui des tkmoins.

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Section: Discussiormsupporting

confidence: 93%

Section: Discussiormmentioning

confidence: 97%

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The Influence of Starvation on Rat Liver Polysomes

Arora¹,

Lamirande²

1971

Can. J. Biochem.

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“…The reports on the intracellular distribution of alkaline phosphatase are somewhat more contradictory. A predominantly microsomal localization of this enzyme was reported for the intestinal mucosa of the rat (Allard, de Lamirande & Cantero, 1957;Triantaphyllopoulos & Tuba, 1959;Robinson, 1963;Ailhaud et al 1963), the calf (Morton, 1954) and the rabbit and guinea pig (Hers, Berthet, Berthet & de Duve, 1951). In contrast, Holt & Miller (1962) had described alkaline phosphatase as a typical brush-border enzyme in the intestinal mucosa ofthe hamster.…”

Section: Discussionmentioning

confidence: 89%

Studies on the fractionation of mucosal homogenates from the small intestine

Hübscher¹,

West²,

Brindley³

1966

Biochemical Journal

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1. Homogenates of the mucosa of the small intestine of the guinea pig were separated by fractional sedimentation into seven different fractions. The enzymic properties of some of these subcellular fractions were compared with those obtained from the mucosa of the small intestine of the rabbit and cat. 2. The enzymic properties of the low-speed sediment (150OOg-min.) were investigated and it was shown that invertase and alkaline ribonuclease were predominantly located in this subcellular fraction, whereas alkaline phosphatase, aryl-amidase, acid phosphatase, acid ribonuclease and phosphoprotein phosphatase, though true constituents of this fraction, occurred to varying degrees in other subcellular structures also. 3. It was shown that the most probable source of the enzymic activities observed in the low-speed sediment was the brush border. Electron micrographs ofthe purified brush-border fraction indicated vesicles derived from the brush-border membrane. 4. A method is described for the fractionation of mucosal homogenates into a brush border-plus-nuclei fraction, a mitochondrial fraction, a microsomal fraction and a particle-free supematant. The fractions were shown to be relatively pure, as indicated by the distribution of invertase, DNA, succinate dehydrogenase, glucose 6-phosphatase and 6-phosphogluconate dehydrogenase. 5. Most of the activity of four lysosomal enzymes present in the nuclei-free homogenate was sedimented at 3750OOg-min., suggesting the occurrence of lysosomal particles in mucosal homogenates. 6. Further fractionation of the microsomal membranes into three fractions is described. The enzymic composition of the membrane fractions is given and discussed in relation to their structure as seen in electron micrographs.The fractionation of homogenates of the mucosa of the small intestine has been described for preparations from the rat (Schmidt,

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“…Laird (1954) has determined the protein and ribonucleic acid distribution in the particulates and soluble fractions of numerous tumours and normal cells and describes distinctive patterns for the neoplasms. It was also well established that the mitochondrial population of pieneoplastic and neoplastic tissues is decreased, due to diminution in number, occasionally in size, and often in structural density of the units (Allard, de Lamirande, and Cantero, 1953). In chemically induced hepatoma the count per cell may be halved, and there is a greater decrease in many individual oxidative enzymes per gram of mitochondrial protein than might be expected from the simple population change.…”

Section: Cytochondria and Carcinogenesismentioning

confidence: 99%

Cytochondrial Aspects of Cellular Pathology

Harman¹

1958

J Clin Pathol

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Behavior of enzymes in liver of starved rats

Cited by 43 publications

References 20 publications

The Influence of Starvation on Rat Liver Polysomes

The Influence of Starvation on Rat Liver Polysomes

Studies on the fractionation of mucosal homogenates from the small intestine

Cytochondrial Aspects of Cellular Pathology

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