trehalase solubilized with 0.5 % triton x-100 and 0.5 % deoxycholate from the brush border membrane of rabbit kidney cortex was all adsorbed on phenyl-sepharose equilibrated with elution buffer containing no detergents , and all the adsorbed enzyme was eluted in one peak on the addition of 0.5 % triton x-100 to the elution buffer , in contrast to the results reported by nakano and sacktor ( j. biochem . 97 , 1329-1335 ( 1985 ] , who separated two forms of trehalase differing in hydrophobicity from rabbit kidney .
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