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* To whom correspondence should be addrcsscd. Step 2・ . To 61 of homogenate, DEAE-cel]ulose (600g, wet wci.oht) pre-equilibruted with 10mM sodium acctate buffer (pH 6,O) was added and thc suspension was stirred gent]y at O"C fbr 3emin, The DEAE-cellu]ose-udsorbcd protein was coilected by suction and washed with 3 1 of thc same bufi'er. then suspendcd in the same buffcr. The column packcd -・ith thc DEAE-cellulose was cluted with a linear grudient ofO 1M NaCl in 11 of the same buffbr. I/ractionsef15mleachwerecollceted.Theenzymeactivity was scpurated inte t",o fractions, the first fraction {tube Nos. 70 99, RNase Le,) and the second fraction (tubc Nos, 1OO-1gO. RNase Le2) were ¢ ollccted (RNase Lei: TA, 610u; SA. I.3ui'mg. RNase Le,, TA, 1300u; SA, O.88ui'mg),

Purification and characterization of a base non-specific and adenylic acid preferring ribonuclease from the fruit bodies of Lentinus edodes.