Abstract
Aqueous dispersions of synthetic phospholipids, in the form of anionic, single bilayer vesicles, were observed to stimulate the appearance of acrosin esterase activity from its zymogen precursor, proacrosin. Enzymatic activity measurements, in parallel with polyacrylamide disc gel electrophoresis in the presence of sodium dodecyl sulfate, indicated that the enzymatic activity produced had resulted from the conversion of proacrosin to acrosin (EC 3.4.21.10), and not from the direct stimulation of a possible proacrosin esterase activity. It is suggested that such bilayer lipid vesicles can be used as a model membrane system to study the activation of proacrosin in vitro.
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- BARTLETT G. R. Phosphorus assay in column chromatography. J Biol Chem. 1959 Mar;234(3):466–468. [PubMed] [Google Scholar]
- BLIGH E. G., DYER W. J. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959 Aug;37(8):911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
- Batzri S., Korn E. D. Single bilayer liposomes prepared without sonication. Biochim Biophys Acta. 1973 Apr 16;298(4):1015–1019. doi: 10.1016/0005-2736(73)90408-2. [DOI] [PubMed] [Google Scholar]
- Cubero Robles E., van den Berg D. Synthesis of lecithins by acylation of O-(sn-glycero-3-phosphoryl) choline with fatty acid anhydrides. Biochim Biophys Acta. 1969 Dec 17;187(4):520–526. doi: 10.1016/0005-2760(69)90049-6. [DOI] [PubMed] [Google Scholar]
- Gitel S. N., Owen W. G., Esmon C. T., Jackson C. M. A polypeptide region of bovine prothrombin specific for binding to phospholipids. Proc Natl Acad Sci U S A. 1973 May;70(5):1344–1348. doi: 10.1073/pnas.70.5.1344. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kassell B., Kay J. Zymogens of proteolytic enzymes. Science. 1973 Jun 8;180(4090):1022–1027. doi: 10.1126/science.180.4090.1022. [DOI] [PubMed] [Google Scholar]
- Kisiel W., Hermodson M. A., Davie E. W. Factor X activating enzyme from Russell's viper venom: isolation and characterization. Biochemistry. 1976 Nov 2;15(22):4901–4906. doi: 10.1021/bi00667a023. [DOI] [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- McRorie R. A., Williams W. L. Biochemistry of mammalian fertilization. Annu Rev Biochem. 1974;43(0):777–803. doi: 10.1146/annurev.bi.43.070174.004021. [DOI] [PubMed] [Google Scholar]
- Meizel S., Mukerji S. K. Proacrosin from rabbit epididymal spermatozoa: partial purification and initial biochemical characterization. Biol Reprod. 1975 Aug;13(1):83–93. doi: 10.1095/biolreprod13.1.83. [DOI] [PubMed] [Google Scholar]
- Morton D. B. Acrosomal enzymes: Immunochemical localization of acrosin and hyaluronidase in ram spermatozoa. J Reprod Fertil. 1975 Nov;45(2):375–378. doi: 10.1530/jrf.0.0450375. [DOI] [PubMed] [Google Scholar]
- Mukerji S. K., Meizel S. Conversion of rabbit testis proacrosin to acrosin. FEBS Lett. 1975 Jun 15;54(2):269–273. doi: 10.1016/0014-5793(75)80090-1. [DOI] [PubMed] [Google Scholar]
- Parrish R. F., Polakoski K. L. Effect of polyamines on the activity of acrosin and the activation of proacrosin. Biol Reprod. 1977 Oct;17(3):417–422. doi: 10.1095/biolreprod17.3.417. [DOI] [PubMed] [Google Scholar]
- Polakoski K. L., McRorie R. A., Williams W. L. Boar acrosin. I. Purification and preliminary characterization of a proteinase from boar sperm acrosomes. J Biol Chem. 1973 Dec 10;248(23):8178–8182. [PubMed] [Google Scholar]
- Polakoski K. L., Parrish R. F. Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J Biol Chem. 1977 Mar 25;252(6):1888–1894. [PubMed] [Google Scholar]
- SCHWERT G. W., TAKENAKA Y. A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta. 1955 Apr;16(4):570–575. doi: 10.1016/0006-3002(55)90280-8. [DOI] [PubMed] [Google Scholar]
- Shinitzky M., Rivnay B. Degree of exposure of membrane proteins determined by fluorescence quenching. Biochemistry. 1977 Mar 8;16(5):982–986. doi: 10.1021/bi00624a027. [DOI] [PubMed] [Google Scholar]
- Stambaugh R., Brackett B. G., Mastroianni L. Inhibition of in vitro fertilization of rabbit ova by trypsin inhibitors. Biol Reprod. 1969 Sep;1(3):223–227. doi: 10.1095/biolreprod1.3.223. [DOI] [PubMed] [Google Scholar]
- WHITAKER J. R., BENDER M. L. KINETICS OF PAPAIN-CATALYZED HYDROLYSIS OF ALPHA-N-BENZOYL-L-ARGININE ETHYL ESTER AND ALPHA-N-BENZOYL-L-ARGININAMIDE. J Am Chem Soc. 1965 Jun 20;87:2728–2737. doi: 10.1021/ja01090a034. [DOI] [PubMed] [Google Scholar]
- Yang S. F., Freer S., Benson A. A. Transphosphatidylation by phospholipase D. J Biol Chem. 1967 Feb 10;242(3):477–484. [PubMed] [Google Scholar]
- Zahler W. L., Doak G. A. Isolation of the outer acrosomal membrane from bull sperm. Biochim Biophys Acta. 1975 Nov 3;406(4):479–488. doi: 10.1016/0005-2736(75)90026-7. [DOI] [PubMed] [Google Scholar]
- Zahler W. L., Polakoski K. L. Benzamidine as an inhibitor of proacrosin activation in bull sperm. Biochim Biophys Acta. 1977 Feb 9;480(2):461–468. doi: 10.1016/0005-2744(77)90038-9. [DOI] [PubMed] [Google Scholar]
- Zaneveld L. J., Robertson R. T., Kessler M., Williams W. L. Inhibition of fertilization in vivo by pancreatic and seminal plasma trypsin inhibitors. J Reprod Fertil. 1971 Jun;25(3):387–392. doi: 10.1530/jrf.0.0250387. [DOI] [PubMed] [Google Scholar]

