X-Message-Number: 12437 Date: Sun, 19 Sep 1999 01:16:09 -0700 (PDT) From: Doug Skrecky <> Subject: stabilization with ethanol and trehalose Authors Mukorah F. Razunguzwa B. Masola B. Institution Department of Biochemistry, University of Zimbabwe, Mount Pleasant, Harare, Zimbabwe. Title Stabilization of rat liver mitochondrial alanine aminotransferase with ethanol and trehalose. Source Cryobiology. 37(4):300-8, 1998 Dec. Abstract Rat liver mitochondrial alanine aminotransferase (mALT) is known to be a very unstable enzyme, a property that has hindered efforts to purify it. In this report we examine the possibility of stabilizing mALT with ethanol, trehalose, and protease inhibitors. The presence of ethanol was shown to slow down the inactivation of mALT, increasing its half-life from 1 to 4 h. Trehalose was found to greatly enhance the stability of mALT in a concentration-dependent manner. In the presence of 36.5% trehalose, the half-life of mALT was 85 h. Of the protease inhibitors tested only antipain and chymostatin slowed down the inactivation of mALT but only within the first 24 h following preparation of the crude enzyme. It is concluded that the inclusion of ethanol and trehalose in purification protocols could aid the purification of the enzyme. It is also concluded that the inclusion of protease inhibitors in purification protocols of mALT may not be necessary as its inactivation does not seem to be due to protease activity. Copyright 1998 Academic Press. Rate This Message: http://www.cryonet.org/cgi-bin/rate.cgi?msg=12437