A paper chromatographic assay for ribonucleases using cyclic mononucleotides as substrates

Nodes, J.T.

doi:10.1016/0006-3002(59)90634-1

Cited by 13 publications

(1 citation statement)

References 11 publications

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“…An alkaline RNase x appears actually to be associated with the mitochondria, while the acid RNase, as well as other acid hydrolases, is said to reside in lysosomes, particles which are morphologically distinct from mitochondria (12). Evidence for the presence of two acid RNases in rat liver has been reported (13). Fewer studies of spleen RNases have been made, the earliest being those of Mayer and Greco, who described some properties of a calf spleen RNase (14,15).…”

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Intracellular Localization of Enzymes in Spleen

Eichel

Roth

1962

The Journal of Cell Biology

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Some properties of rat spleen ribonuclease have been studied, and the intracellular distribution of the enzyme and ribonucleic acid have been presented. Spleen ribonuclease exhibits maximal activity at pH 5.8, and although there is some evidence for the presence of an enzyme with an optimum at pH 7.0, it is not conclusive. The enzyme is concentrated primarily in the mitochondrial fraction, but significant quantities occur in the supernatant fluid. The latter contains ribonuclease inhibitor similar to that found in liver. The effects of whole body x-irradiation, magnesium ion, substrate concentration, type of buffer, presence of p-chloromercuriphenylsulfonic acid, deoxycholate, and Triton X-100 on ribonuclease activity are examined.

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confidence: 99%