The amino terminal sequences of boar sperm proacrosin and active acrosin are identical
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. Isolierung eines Trypsin-ähnlichen Enzyms (Akrosin) aus Eberspermien
2. N-Terminal Amino Acid Sequence of Boar Sperm Acrosin. Homology with Other Serine Proteinases
3. Spectroscopic Determination of Tryptophan and Tyrosine in Proteins*
4. Boar Acrosin. Isolation of Two Active Forms from Boar Ejaculated Sperm
5. Multiple Forms of Boar Acrosin and their Relationship to Proenzyme Activation
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Isolation and partial characterization of boar proacrosin;Collection of Czechoslovak Chemical Communications;1990
2. Activation of boar proacrosin is effected by processing at both N-and C-terminal portions of the zymogen molecule;FEBS Letters;1989-02-13
3. Boar proacrosin is a single-chain molecule which has the N-terminus of the acrosin A-chain (light chain);FEBS Letters;1988-12-05
4. Immunological approach to characterize proacrosin and various acrosin forms in boar and man by monoclonal antibodies;Gamete Research;1987-12
5. Purification and Initial Characterization of Proacrosins from Guinea Pig Testes and Epididymal Spermatozoa1;Biology of Reproduction;1987-08-01
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