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THE EFFECTS OF RIBONUCLEASE ON THE RIBONUCLEIC ACID AND ENZYME ACTIVITIES OF MICROSOMES ISOLATED FROM RAT LIVER HOMOGENATES
Author(s) -
Alex B. Novikoff,
JEAN RYAN,
Estelle Podber
Publication year - 1954
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/2.5.401
Subject(s) - biochemistry , ribonuclease , microsome , acid phosphatase , rna , enzyme , digestion (alchemy) , chemistry , alkaline phosphatase , biology , microbiology and biotechnology , chromatography , gene
1. The RNA of isolated rat liver microsomes is readily accessible to ribonuclease digestion. About 85% of the RNA-ribose is removed by the nuclease; data in the literature suggest that the rest remains in smaller polynucleotides rather than RNA per se. 2. Digestion of microsomes with ribonuclease dissolved in glycyl-glycine buffer, pH 7.0, has no effect upon the activities of the enzymes studied: glucose-6-phosphatase, esterase, triacetic acid lactonase, adenosine-5'-phosphatase, acid phosphatase, adenosine triphosphatase, and succinoxidase. 3. Digestion with ribonuclease dissolved in water has no effect upon the acid phosphatase and adenosine-5'-phosphatase activities, while esterase, adenosine triphosphatase and succinoxidase activities are somewhat lower. Glucose-6-phosphatase activity is markedly reduced, as it is by incubation of microsomes with either water or buffer alone.

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