Monoclonal antibodies to bovine and human acrosin

1986 ◽  
Vol 64 (12) ◽  
pp. 1242-1248 ◽  
Author(s):  
John S. Elce ◽  
Elise J. Graham ◽  
Gizela Zboril ◽  
Lisette Leyton ◽  
Elcira Perez ◽  
...  

Monoclonal antibodies to human acrosin were required for studies of immunological interference with fertilization. Since human acrosin was not available in adequate amounts, monoclonal antibodies have been raised in mice against purified bovine acrosin and screened for cross-reaction with human sperm cells. Two of these antibodies are described, B4F6 and C2E5. Data from enzyme-linked immunosorbent assays, immunoblots, immunoprecipitation, and indirect immunofluorescence on sperm cells indicate that B4F6 binds only to bovine acrosin, and that C2E5 binds both to bovine and to human acrosin at a conformationally determined epitope. The antibodies do not inhibit the hydrolysis of benzoylarginine ethyl ester by acrosin, but C2E5 did inhibit the dissolution of the hamster zona pellucida by purified human acrosin. The antibodies have also been used for affinity purification of acrosin and proacrosin.

1981 ◽  
Vol 91 (1) ◽  
pp. 175-183 ◽  
Author(s):  
F G Falkner ◽  
H Saumweber ◽  
H Biessmann

Monoclonal antibodies were prepared against a 46,000 mol wt major cytoplasmic protein from Drosophila melanogaster Kc cells. These antibodies reacted with the 46,000 and a 40,000 mol wt protein from Kc cells. Some antibodies showed cross-reaction with 55,000 (vimentin) and 52,000 mol wt (desmin) proteins from baby hamster kidney (BHK) cells that form intermediate sized filaments in vertebrate cells. In indirect immunofluorescence, the group of cross reacting antibodies stained a filamentous meshwork in the cytoplasm of vertebrate cells. In Kc cells the fluorescence seemed to be localized in a filamentous meshwork that became more obvious after the cells had flattened out on a surface. These cytoskeletal structures are heat-labile; the proteins in Kc or BHK cells rearrange after a brief heat shock, forming juxtanuclear cap structures.


1991 ◽  
Vol 19 (3) ◽  
pp. 269-285 ◽  
Author(s):  
Mary Condon Mahony ◽  
David L. Fulgham ◽  
Peter F. Blackmore ◽  
Nancy J. Alexander

2002 ◽  
Vol 10 (7) ◽  
pp. 2171-2175 ◽  
Author(s):  
Zhen-Dan Shi ◽  
Bing-Hui Yang ◽  
Jing-Jing Zhao ◽  
Yu-Lin Wu ◽  
Yong-Yong Ji ◽  
...  

1991 ◽  
Vol 73 (2-3) ◽  
pp. 23a-23a
Author(s):  
Gwenola Lannic ◽  
Georges Katsanis ◽  
Eric Vendrely ◽  
Philippe Chevaillier ◽  
Jean-Pierre Daddune

2007 ◽  
Vol 19 (2) ◽  
pp. 392 ◽  
Author(s):  
Stephanie Singleton ◽  
Olga Mudrak ◽  
Mahmood Morshedi ◽  
Sergio Oehninger ◽  
Irina Zalenskaya ◽  
...  

During the process of mammalian spermiogenesis, a significant reorganisation of the chromatin structure occurs involving the sequential substitution of somatic histones with protamines. In the human sperm nucleus, ~15% of the basic nuclear protein complement is maintained as histones. Human testis/sperm-specific histone H2B (hTSH2B) is a variant of the histone H2B expressed exclusively in spermatogenic germline cells and present in some mature sperm cells. Thus, this protein marks a subpopulation of sperm cells in the ejaculate. Using indirect immunofluorescence, we examined the influence of hTSH2B on zona pellucida binding and sperm head decondensation in amphibian egg cell-free extract. As suggested by previous studies, we found that hTSH2B can be localised in only ~30% of sperm cells within a given ejaculate. We established that the presence of hTSH2B does not influence sperm zona pellucida binding capacity. Finally, we found that decondensation occurred more rapidly and to a greater extent in those cells containing hTSH2B. We propose that the presence or absence of hTSH2B within spermatozoa influences pronuclei formation and the activation of paternal genes following fertilisation and during early embryonic development.


1997 ◽  
Vol 12 (Suppl_2) ◽  
pp. 290-291
Author(s):  
M. van Duin ◽  
A. Grootenhuis ◽  
H. Bunschoten ◽  
R.J. Aitken

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