Boar proacrosin is a single-chain molecule which has the N-terminus of the acrosin A-chain (light chain) |
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Authors: | D Cechová E T?pfer-Petersen A Henschen |
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Affiliation: | Max Planck Institute for Biochemistry, Martinsried, FRG. |
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Abstract: | 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. |
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