TL;DR: The results demonstrate that acrosin-liposome binding is due in part to electrostatic charge interactions and indicate that the enzyme has properties of an extrinsic membrane protein.
TL;DR: Proacrosin interacts with mannose residues through binding sites located at both the N- and C-terminal portion of the protein, and the full-length protein is required for maximal BSA-mannose binding, and binding sites are stabilized by noncovalent bonds and by disulfide linkages.
TL;DR: Comparison of the structure-activity relationships for the inhibition of acrosin and trypsin showed differences in the binding sites of both enzymes.
Abstract: A series of substituted benzamidines was tested for their inhibitory effects on boar acrosin. Substituents with electron-donating properties and small aliphatic residues increase the inhibitory activity of benzamidine, whereas aromatic residues have only a slight enhancing influence. Only substituents with a beta- or gamma-keto group increase the acrosin binding affinity by more than one order of magnitude. Comparison of the structure-activity relationships for the inhibition of acrosin and trypsin showed differences in the binding sites of both enzymes.