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Studies on ram acrosin ec activation of pro acrosin accompanying the isolation of acrosin from spermatozoa and purification of the enzyme by affinity chromatography

Studies on ram acrosin ec activation of pro acrosin accompanying the isolation of acrosin from spermatozoa and purification of the enzyme by affinity chromatography

Biochemical Journal 175(1): 227-238

A previously described, freeze-dried, partially purified ram acrosin [EC] preparation was fractionated on a column of Sepharose linked to the acrosin inhibitor p-(p'-aminophenoxypropoxy)benzamidine. Two acrosin fractions were obtained. .beta.-Acrosin was homogeneous, quite stable at low pH and very stable when freeze-dried. Its MW is about 38,000, and it contains about 6 sugar residues/molecule, but no sialic acid. .psi.-Acrosin consisted of at least 3 unstable forms of acrosin. When the entire purification process, starting from collection of semen, was carried out as rapidly as possible, the yield of .beta.-acrosin was increased and very little .psi.-acrosin was obtained. In fresh ram semen the acrosin is present as the intra-acrosomal zymogen, proacrosin. After its extraction from spermatozoa autoproteolytic reactions convert proacrosin into .beta.-acrosin; .psi.-acrosin appears to be breakdown products of .beta.-acrosin. When .beta.-acrosin was passed through a column of Sepharose linked to the non-inhibitory deamidinated analog of the inhibitor it behaved as a hydrophobic protein. This is consistent with the view that acrosin (as zymogen) occurs in spermatozoa as a membrane-bound protein. Success in the isolation of pure acrosin in high yield calls for an affinity adsorbent with the appropriate subsidiary hydrophobic properties.

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Accession: 006511579

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