Partial characterization of a proacrosin binding protein.
All of the acid (pH 4.0) extracted proacrosin from porcine epididymal spermatozoa was found to be tightly associated with a specific protein referred to as the binding protein. A combination of gel filterations and gel electrophoresis revealed that the binding protein is composed of a major 28 kd and a minor 29 kd protein. Both of the proteins were shown to be nonproteolytic by gelatin SDS-PAGE analysis and the amino acid composition analysis of the purified 28 kd protein revealed that it is not related to the proteolytic component of the proacrosinacrosin system.
Yi
L S
LS
Department of Obstetrics and Gynecology, Washington University School of Medicine, St Louis, MO 63110.
Runion
C M
CM
Willand
J L
JL
Polakoski
K L
KL
D000176:Acrosin / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004792:Enzyme Precursors / Q000378:metabolism*; D004822:Epididymis; D008297:Male; D008970:Molecular Weight; D013094:Spermatozoa / Q000378:metabolism*; D013552:Swine
D000596:Amino Acids; D002352:Carrier Proteins; D004792:Enzyme Precursors; C022438:proacrosin; D000176:Acrosin