Satoh_1995_Toxicol.Lett_82-83_439

Reference

Title : Molecular aspects of carboxylesterase isoforms in comparison with other esterases - Satoh_1995_Toxicol.Lett_82-83_439
Author(s) : Satoh T , Hosokawa M
Ref : Toxicol Lett , 82-83 :439 , 1995
Abstract :

The involvement of carboxylesterase, acetylcholinesterase, butyrylcholinesterase and cholesterol esterase in pharmacology and toxicology are well recognized. However, there are few papers concerning the comparative studies of these serine hydrolases in terms of molecular level. Recently, we have studied various aspects of carboxylesterases using cDNAs of carboxylesterase isozymes purified from 9 animal species and human liver microsomes, and found that there is high homology of the N-terminal amino acid sequences of the isozymes tested. On the other hand, we compared the amino acid sequences at the active site of the individual esterases and found that the sequences of all esterases tested are strictly conserved. These results strongly suggest that the esterases involved are classified into the serine hydrolase super family.

PubMedSearch : Satoh_1995_Toxicol.Lett_82-83_439
PubMedID: 8597091
Gene_locus related to this paper: human-CES1 , ratno-lmcxe , ratno-q68g49

Related information

Gene_locus human-CES1    ratno-lmcxe    ratno-q68g49

Citations formats

Satoh T, Hosokawa M (1995)
Molecular aspects of carboxylesterase isoforms in comparison with other esterases
Toxicol Lett 82-83 :439

Satoh T, Hosokawa M (1995)
Toxicol Lett 82-83 :439