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Two forms of basic trypsin-like arginine amidases in boar sperm
T Kobayashi1, Y Matsuda, S Oshio
1Department of Obstetrics and Gynecology, School of Medicine, Keio University, Tokyo, Japan.
Archives of Andrology
|January 1, 1993
Summary
Researchers separated two boar sperm enzymes, acrosin and basic arginine amidase, using affinity adsorption. Differences in their properties and binding to lima bean trypsin inhibitor (LBTI) enabled their distinct separation.
Area of Science:
- Biochemistry
- Enzymology
- Reproductive Biology
Background:
- Boar sperm contain enzymes crucial for fertilization.
- Acrosin is a well-known sperm enzyme, but other related amidases may exist.
- Understanding these enzymes is key to reproductive processes.
Purpose of the Study:
- To isolate and characterize acrosin and a newly detected basic arginine amidase from boar sperm.
- To differentiate these enzymes based on their biochemical properties and inhibitor interactions.
- To explore the utility of affinity adsorption for enzyme separation.
Main Methods:
- Affinity adsorption chromatography was employed for enzyme separation.
- Lima bean trypsin inhibitor (LBTI) and aprotinin columns were used for selective binding.
- Enzymes were characterized by their response to calcium chloride, substrate specificity, and inhibitor interactions.
Main Results:
- Acrosin and a novel basic arginine amidase were successfully separated using LBTI and aprotinin columns, respectively.
- The two enzymes exhibited distinct responses to calcium chloride and varying substrate specificities.
- Significant differences in affinity for LBTI were observed, facilitating their separation.
Conclusions:
- Boar sperm possess at least two distinct basic arginine amidases, including acrosin.
- Differences in enzyme-inhibitor affinity, particularly with LBTI, are effective for separating these amidases.
- This study provides a method for differentiating key sperm enzymes.