N-Terminal Amino Acid Sequence of Boar Sperm Acrosin. Homology with Other Serine Proteinases
Author:
Publisher
Walter de Gruyter GmbH
Subject
Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/bchm2.1980.361.2.1823/pdf
Reference10 articles.
1. Evidence for the role of a trypsin-like enzyme in the hamster sperm acrosome reaction
2. Inhibition of in Vitro Fertilization of Rabbit Ova by Trypsin Inhibitors
3. Cleavage Specificity of Boar Acrosin on Polypeptide Substrates, Ribonuclease and Insulin B-Chain
4. Inactivation of Boar Acrosin by Peptidyl-arginyl-chloromethanes Comparison of the Reactivity of Acrosin, Trypsin and Thrombin
5. Purification and Properties of Boar Acrosin
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1. Purification, Characterization, and N-Terminal Amino Acid Sequence of the Adenylyl Cyclase-Activating Protease from Bovine Sperm1;Biology of Reproduction;1995-03-01
2. Rat sperm acrosin: cDNA sequence, derived primary structure and phylogenetic origin;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1991-10
3. Specific binding of sulphated polymers to ram sperm proacrosin;FEBS Letters;1990-09-17
4. Zona pellucida-binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin B-chain (heavy chain);FEBS Letters;1990-06-04
5. Zona pellucida induces conversion of proacrosin to acrosin;International Journal of Andrology;1990-06
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