A nuclease from mung bean sprouts

A nuclease from mung bean sprouts

1962

REP.MB-1068

A nuclease from mung bean sprouts has been purified approximately 2000-fold. At this stage of purification th nuclease shows no specificity toward the sugar moiety and hydrolyzes ribonucleic acid and deoxyribonucleic acid at approximately the same rate. The predominant action of the enzyme is endonucleolytic. The products range from mononucleotides to at least heptanucleotides. Deoxyadenylic acid represents approximately three-quarters of all the mononucleotides formed from deoxyribonucleic acid. No definite end point of the reaction could be established. All products are terminated in 5'-phosphate and 3'-hydroxyl. The enzyme shows a pronounced preference toward the d-pA-pX linkage (d-pA denotes 5'-phosphate of adenosine; pX, 5'-phosphate of nucleoside of unknown composition). The enzyme is capable of hydrolyzing some dinucleotides to mononucleotides, d-pApA being most susceptible.

v.237(2):506-511, JOURNAL OF BIOLOGICAL CHEMISTRY

Research > Published Articles