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.

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