Abstract:
:A mixture of 55 and 53 kDa boar proacrosins was autoactivated at pH 8.5 to produce a 43 kDa intermediate form and a 35 kDa mature acrosin, and each of four forms of (pro)acrosins was isolated. Analysis of the N-terminal sequences of the two proacrosins indicated the existence of a segment corresponding to the acrosin light chain at the N-terminal end of the zymogen. Two N-terminal sequences identical with those of the light and heavy chains were found in the intermediate form and mature acrosin. The proacrosins and the intermediate contained many more proline residues than the mature enzyme. These results indicate that the activation of boar acrosin zymogen is achieved by the removal of a C-terminal segment rich in proline residues and by the cleavage of the Arg23-Val24 bond leading to the formation of the light and heavy chains.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Baba T,Michikawa Y,Kawakura K,Arai Ydoi
10.1016/0014-5793(89)81178-0subject
Has Abstractpub_date
1989-02-13 00:00:00pages
132-6issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(89)81178-0journal_volume
244pub_type
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