title: [An arginine esterase in the human sperm].
abstract: Human sperm was highly purified by the use of a discontinuous Percoll density gradient placed in an innercolumn of a centrifugation tube. Seminal plasma contamination was only 0.0008 percent in the purified sperm. A new basic arginine ester hydrolyzing enzyme with a weak affinity for lima bean trypsin inhibitor (LBTI) Cellulofine column was found in the purified human sperm, and the characteristics of this enzyme were found to be different from those of human acrosin.
authors.forename: Y
authors.initials: Y
authors.lastname: Matsuda
authors.forename: S
authors.initials: S
authors.lastname: Oshio
authors.forename: S
authors.initials: S
authors.lastname: Kaneko
authors.forename: R
authors.initials: R
authors.lastname: Iizuka
authors.forename: H
authors.initials: H
authors.lastname: Mohri
authors.forename: S
authors.initials: S
authors.lastname: Akihama
mesh_terms: D002122:Calcium Chloride / Q000494:pharmacology; D002265:Carboxylic Ester Hydrolases / Q000032:analysis* / Q000378:metabolism; D006801:Humans; D008297:Male; D013094:Spermatozoa / Q000201:enzymology*
chemical_list: C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases; D002122:Calcium Chloride