The phospholipase A2 of human spermatozoa; purification and partial sequence.
In view of its proposed key role in the acrosome reaction, phospholipase A2 has been isolated and purified from human spermatozoa. Following SDS-PAGE, a single major band was obtained with an estimated molecular mass of 16.7 kDa. Sequence analysis of the N-terminal portion of the molecule revealed the identity of the first 19 amino acids to be YNYQFGLMIVITKGHFAMV. From this partial analysis it is evident that the phospholipase A2 of human spermatozoa represents a new sequence. Of interest is the location of glutamine-4, phenylalanine-5, methionine-8 and isoleucine-9; this sequence appears to be highly conserved throughout evolution.
Langlais
J
J
Maisonneuve-Rosemont Hospital Research Center, University of Montreal, Canada.
Chafouleas
J G
JG
Ingraham
R
R
Vigneault
N
N
Roberts
K D
KD
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007202:Indicators and Reagents; D007700:Kinetics; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010741:Phospholipases A / Q000235:genetics* / Q000302:isolation & purification* / Q000378:metabolism; D054467:Phospholipases A2; D012689:Sequence Homology, Nucleic Acid; D013094:Spermatozoa / Q000201:enzymology*
D007202:Indicators and Reagents; D010741:Phospholipases A; D054467:Phospholipases A2