Boar proacrosin is a single-chain molecule which has the N-terminus of the acrosin A-chain (light chain).
Boar proacrosin was isolated from spermatozoa by a novel procedure under conditions preventing proenzyme activation. The spermatozoal extract was fractionated by gel filtration and reversed-phase FPLC, all in acidic solutions. Isolated proacrosin had a molecular mass of 55/53 kDa (doublet) and was devoid of amidolytic activity. Its single N-terminal sequence corresponded to that of the 23-residue acrosin A-chain and continued with that of the acrosin B-chain. Autoactivation at pH 7.8 did not influence the molecular mass. However, activated material contained two parallel N-terminal sequences, those of the A- and B-chain. Thus, activation of proacrosin is analogous to that of other serine proteinase proenzymes.
D000176:Acrosin / Q000302:isolation & purification* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000302:isolation & purification* / Q000378:metabolism; D046911:Macromolecular Substances; D008297:Male; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000302:isolation & purification*; D013094:Spermatozoa / Q000201:enzymology; D013552:Swine
D004792:Enzyme Precursors; D046911:Macromolecular Substances; D012697:Serine Endopeptidases; C022438:proacrosin; D000176:Acrosin