Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.21.3 (deoxyribonuclease)
 1,528 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Partially purified bacterial extracts were prepared from segregated stalked and swarmer bacteria of Caulobacter crescentus and assayed for ATP-dependent deoxyribonuclease activity. This activity was found to be very low in the swarmer bacteria compared with a pure population of stalked cells or an asynchronous population of C. crescentus.
J Gen Microbiol 1980 Dec
PMID:Short communication: ATP-dependent deoxyribonuclease activity in segregated cell types of Caulobacter crescentus. 1984 61

A procedure is described for the purification of salmon testis deoxyribonuclease II by means of acid extraction, fractional precipitation with ammonium sulfate, heat denaturation of extraneous proteins, and ethanol fractionation. This process separates the deoxyribonuclease activity from that of ribonuclease, phosphatase, phosphodiesterase, and protease. Over 50 per cent of the activity is retained with an over-all enrichment of 20,000-fold. The enzyme degrades both native and heat-denatured DNA, but the rate of degradation of the latter is only one-tenth that of the former. It does not hydrolyze apurinic acid. The enzyme is most stable in the pH range 4 to 5. Electrolytes are essential for the expression of its activity: monovalent ions satisfy the requirement, but divalent ones are much more effective. Above a certain optimum concentration, each electrolyte is inhibitory. The pH of maximal activity, under conditions of optimal ionic strength, is 4.8; the temperature optimum is near to 55 degrees C.
J Gen Physiol 1962 Mar 01
PMID:Deoxyribonuclease from Salmon Testes : I. Purification and properties. 1987 45


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