Two forms of basic trypsin-like arginine amidases in boar sperm.
Acrosin and newly detected basic arginine amidase were separated from boar sperm by affinity adsorption using lima bean trypsin inhibitor (LBTI) and aprotinin columns, respectively. These enzymes differed in various respects, including response against calcium chloride, amidolytic substrate specificity, and reaction against the inhibitor. They also differed widely in the affinity to LBTI. The difference appears to be expressed as the difference in ability of affinity of the enzymes with LBTI, thus leading to their separation.
Kobayashi
T
T
Department of Obstetrics and Gynecology, School of Medicine, Keio University, Tokyo, Japan.
Matsuda
Y
Y
Oshio
S
S
Kaneko
S
S
Hara
I
I
Umeda
T
T
Nozawa
S
S
Akihama
S
S
D000176:Acrosin / Q000032:analysis; D000581:Amidohydrolases / Q000032:analysis* / Q000037:antagonists & inhibitors; D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000378:metabolism; D001120:Arginine / Q000378:metabolism*; D002122:Calcium Chloride / Q000494:pharmacology; D008297:Male; D008969:Molecular Sequence Data; D013094:Spermatozoa / Q000201:enzymology*; D013379:Substrate Specificity; D013552:Swine; D014361:Trypsin Inhibitors / Q000378:metabolism
D014361:Trypsin Inhibitors; D007611:Aprotinin; D001120:Arginine; D000176:Acrosin; D000581:Amidohydrolases; D002122:Calcium Chloride