Substrate specificity of a human-specific esterase

✍ Scribed by Devidayal Munjal; Noel R. Rose

• Book ID: 102984118
• Publisher: Elsevier Science
• Year: 1973
• Tongue: English
• Weight: 729 KB
• Volume: 54
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(73)90380-1

✦ Synopsis

A human species-specific esterase has been identified in tissues. cell cultures, and urine. It is the most slowly migrating (i.e., cathodal) of the e&erase isoenzymes in agarose electrophoresis; it is not a choline estrase, a pseudocholine e&erase, an acetyl phenylalanine&naphthyl esterase or Nbenzoyl-arginine-3-naphthyl esterase. Hydrolysis of N-methyl indoxyl acetate caused by this esterase is not inhibited by eserine, eserine sulfate, or EDTA. Phenylmethylsulfonyl fluoride, however, did inhibit hydrolysis. Furthermore, this cathodal e&erase does not show any chymotrypsin, trypsin, or leucine aminopeptidase enzyme activity.