Abstract
1. 1. Nα-Acetylhistidine deacetylase was purified from the brain of rainbow trout to apparent homogeneity. 2. 2. The brain and eye deacetylases are the same metalloenzyme which is a dimeric protein with a subunit of 55 kDa. 3. 3. The deacetylase showed strong activity against Nα- chloroacetyl- l- leucine and glycyl- l-leucine. Anserine, carnosine and homocarnosine were poorer substrates than Nα- acetyl- l- histidine and tripeptides tested were unable to be hydrolyzed. 4. 4. High activity of the deacetylase was found in all regions of the trout brain except for the spinal cord and the optic nerve. In subcellular fractionation, 90% of the total deacetylase activity was recovered in the soluble supernatant fraction, whereas a large proportion (40%) of the total endogenous acetylhistidine occurred in the crude mitochondrial pellet.
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