Zobrazeno 1 - 8
of 8
pro vyhledávání: '"J W Straus"'
Autor:
K L Polakoski, J W Straus
Publikováno v:
Biochemical Journal. 201:657-660
Proacrosin, the zymogen precursor of acrosin, was shown to associate with anionic phospholipid membranes through apparent electrostatic charge interactions. This association was diminished by elevated cation concentrations and was dependent on membra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12467a3b9b36037d9115228a24fcc617
https://doi.org/10.1042/bj2010657
https://doi.org/10.1042/bj2010657
Publikováno v:
Journal of Biological Chemistry. 256:5662-5668
Acrosin, an enzyme required for fertilization, is an endogenous proteinase associated with membranes of the sperm acrosome. Liposomes were utilized as a model system to evaluate the mode of association between highly purified boar acrosin and phospho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::740c3678bbd8c9a07e63133dd1bad4c3
https://doi.org/10.1016/s0021-9258(19)69256-2
https://doi.org/10.1016/s0021-9258(19)69256-2
Autor:
K L Polakoski, J W Straus
Publikováno v:
Journal of Biological Chemistry. 257:7962-7964
Acrosin is an extrinsic membrane proteinase from spermatozoa which functions in the fertilization process. Liposomes were utilized as a model system to determined possible effects of membrane association on acrosin's enzymatic activity. By comparison
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36b321773d7710f951d0ecfc3e6b19b4
https://doi.org/10.1016/s0021-9258(18)34281-9
https://doi.org/10.1016/s0021-9258(18)34281-9
Publikováno v:
Methods in enzymology. 101
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::11be8932fe1c09ccd7f71da381e44b5c
https://pubmed.ncbi.nlm.nih.gov/6888279
https://pubmed.ncbi.nlm.nih.gov/6888279
Autor:
J W, Straus, K L, Polakoski
Publikováno v:
The Journal of biological chemistry. 257(14)
Acrosin is an extrinsic membrane proteinase from spermatozoa which functions in the fertilization process. Liposomes were utilized as a model system to determined possible effects of membrane association on acrosin's enzymatic activity. By comparison
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4cd1024bd1715bf8c8ee50d12f44f8fe
https://pubmed.ncbi.nlm.nih.gov/7045116
https://pubmed.ncbi.nlm.nih.gov/7045116
Autor:
Kenneth L. Polakoski, J. D. Geratz, John D. Paulson, Richard F. Parrish, Richard R. Tidwell, J. W. Straus, F. M. Stevens
Publikováno v:
Journal of medicinal chemistry. 21(11)
A series, consisting of 52 benzamidine derivatives, was evaluated for inhibitory activity against homogeneous boar sperm acrosin. All of the compounds in the series proved to be more potent than benzamidine (Ki = 4.0 x 10(-6) M), with one of the deri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f717bb4346aafb5de62596229ef6c4e
https://pubmed.ncbi.nlm.nih.gov/722718
https://pubmed.ncbi.nlm.nih.gov/722718
Autor:
Kenneth L. Polakoski, J. W. Straus, Richard F. Parrish, J. D. Geratz, John D. Paulson, Richard R. Tidwell, F. M. Stevens
Publikováno v:
Chemischer Informationsdienst. 10
A series, consisting of 52 benzamidine derivatives, was evaluated for inhibitory activity against homogeneous boar sperm acrosin. All of the compounds in the series proved to be more potent than benzamidine (Ki = 4.0 x 10(-6) M), with one of the deri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::882454c7ebc99921d79a625af817d755
https://doi.org/10.1002/chin.197912204
https://doi.org/10.1002/chin.197912204
Autor:
J E, Robbers, J W, Straus
Publikováno v:
Lloydia. 38(4)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::86bff93252d5509b9bd81287f8315c43
https://pubmed.ncbi.nlm.nih.gov/1186436
https://pubmed.ncbi.nlm.nih.gov/1186436