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Boar acrosin is a two-chain molecule. Isolation and primary structure of the light chain; homology with the pro-part of other serine proteinases

Data up to Jan 2025

Published1984
Citations39
References31

Total Citations Per Year

Abstract

References (31)

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Purification and Properties of Boar Acrosin

1980 • 41 citations

Boar malpha-acrosin. Purification and characterization of the inital active enzyme resulting from the conversion of boar proacrosin to acrosin.

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Boar Acrosin. Isolation of Two Active Forms from Boar Ejaculated Sperm

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Evidence for an intrazymogen mechanism in the conversion of proacrosin into acrosin

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A New Acrosin Inhibitor from Boar Spermatozoa

1982 • 26 citations

N-Terminal Amino Acid Sequence of Boar Sperm Acrosin. Homology with Other Serine Proteinases

1980 • 24 citations

Proacrosin conversion inhibitor. Purification and initial characterization of a boar sperm protein which prevents the conversion of proacrosin into acrosin.

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Oligomerisation of Boar Acrosin

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Boar acrosin is a two-chain molecule. Isolation and primary structure of the light chain;… (1984) – European Journal of Biochemistry | Metascience Observatory Explorer