Studies on ram acrosin. Isolation from spermatozoa, activation by cations and organic solvents, and influence of cations on its reaction with inhibitors.

The Biochemical Journal
C R BrownE F Hartree

Abstract

1. A simple method is given for isolating from ram spermatozoa a water-soluble form of acrosin (a trypsin-like enzyme) which is about 25% pure. It is free from an acrosin inhibitor which is located in the spermatozoa. 2. In the hydrolysis of N-alpha-benzoyl-l-arginine ethyl ester the degree of activation of acrosin by Ca(2+), and by some other cations, is dependent on the extent of contamination by the inhibitor. In 50mm-Tris-HCl buffer (pH8.2) activation by Ca(2+) did not exceed 40%, but acrosin that is partially inhibited may be activated by up to 300%: this is due to cation-mediated protection of acrosin against the inhibitor. 3. Increasing concentrations of buffers (e.g. Tris) also activate acrosin but at above certain buffer concentrations Ca(2+) no longer exerts an activating effect and may become inhibitory. Ca(2+) is also inhibitory when added to assay systems involving anionic buffers with chelating properties. This is due to a fall in pH. 4. The above results suggest reasons for conflicting conclusions in papers dealing with the effects of Ca(2+) on acrosin activity. 5. Inhibition of acrosin by the Kunitz pancreatic trypsin inhibitor is increased on addition of Ca(2+). Inhibitions of trypsin by the acrosin inhibitor a...Continue Reading

Citations

Nov 1, 1987·The Journal of Experimental Zoology·C E Arboleda, G L Gerton
Nov 1, 1992·Biological Reviews of the Cambridge Philosophical Society·E R RoldanA D Vitullo
Mar 19, 1999·The Journal of Veterinary Medical Science·E KawakamiI Oishi
May 5, 1981·Biochimica Et Biophysica Acta·S K Bhatnagar, S R Anand
Nov 22, 1983·Biochimica Et Biophysica Acta·Y Marushige, K Marushige
Jun 22, 1978·Biochimica Et Biophysica Acta·Y Marushige, K Marushige
Sep 11, 1978·Biochimica Et Biophysica Acta·C R Brown, R A Harrison
Apr 7, 1988·Biochimica Et Biophysica Acta·P Ben-AvH Breitbart

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