Boar sperm proacrosin infrared investigation: Secondary structure analysis after autoactivation and suramin binding

Biochemical and Molecular Medicine

Volumn 58, Issue 1, 1996, Pages 37-45

  Fini, Carlo ^a   Tanfani, Fabio ^b   Bertoli, Enrico ^b   Jansen, Stephan ^c   Spicer, Carl ^c   Floridi, Ardesio ^a   Jones, Roy ^c  

^a UNIVERSITY OF PERUGIA   (Italy)

^b UNIVERSITÀ POLITECNICA DELLE MARCHE   (Italy)

^c BABRAHAM INSTITUTE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PROACROSIN; SURAMIN;

ANIMAL CELL; ARTICLE; CELL ADHESION; FOURIER TRANSFORMATION; INFRARED SPECTROPHOTOMETRY; MALE; NONHUMAN; PROTEIN DENATURATION; PROTEIN SECONDARY STRUCTURE; SEMEN ANALYSIS; THERMAL ANALYSIS;

EID: 0030175750     PISSN: 10773150     EISSN: None     Source Type: Journal    
DOI: 10.1006/bmme.1996.0030     Document Type: Article

References (32)

1. 1. Meizel S. The importance of hydrolytic enzymes to an exocytotic event, the mammalian sperm acrosome reaction. Biol Rev 59:125-157, 1984.
2. 2. Adham IM, Klemm U, Maier W-M, Hoyer-Fender S, Tsaousidou S, Engel W. Molecular cloning of preproacrosin and analysis of its expression pattern in spermatogenesis. Eur J Biochem 182:563-568, 1989.
3. 3. Baba T, Kashiwabara S, Watanabe K, Itoh H, Michikawa Y, Kimura K, Takada M, Fukamizu A, Arai Y. Activation and maturation mechanisms of boar acrosin zymogen based on the deduced primary structure. J Biol Chem 264:11920-11927, 1989.
4. 4. Klemm U, Flake A, Engel W. Rat sperm acrosin: cDNA sequence, derived primary structure and phylogenetic origin. Biochim Biophys Acta 1090:270-272, 1991.
5. 5. Jones R. Identification and functions of mammalian sperm-egg recognition molecules during fertilization. J Reprod Fertil Suppl 42:85-105, 1990.
6. 6. Jones R. Interaction of zona pellucida glycoproteins, sulphated carbohydrates and synthetic polymers with proacrosin, the putative egg-binding from mammalian spermatozoa. Development 111:1155-1163, 1991.
7. 7. Urch UA, Patel H. The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulphated polysaccharides. Development 111:1165-1172, 1991.
8. 8. Hawking F. Suramin: With special reference to onchocerciasis. Adv Pharmacol Chemother 15:289-322, 1978.
9. 9. La Rocca RV, Stein CA, Myers CE. Suramin-prototype of a new generation of antitumor compounds. Cancer Cells 2:107-115, 1990.
10. 10. Polakoski KL, Parrish RF. Boar proacrosin. Purification and preliminary activation studies of proacrosin isolated from ejaculated boar sperm. J Biol Chem 252:1888-1894, 1977.
11. 11. Lo Leggio L, Williams RM, Jones R. Some effects of zona pellucida glycoproteins and sulphated polymers on the autoactivation of boar sperm proacrosin and activity of β-acrosin. J Reprod Fertil 100:177-185, 1994.
12. 12. Salomaa P, Schaleger LL, Long FA. Solvent deuterium isotope effect on acid-base equilibria. J Am Chem Soc 86:1-7, 1964.
13. 13. Kauppinen JK, Moffat DS, Mantsch HH, Cameron DG. Fourier self-deconvolution: A method for resolving intrinsically overlapped bands. Appl Spectrosc 35:271-276, 1981.
14. 14. Banecki B, Zylicz M, Bertoli E, Tanfani F. Structural and functional relationships in DnaK and DnaK756 heat-shock proteins fron Escherichia coli. J Biol Chem 267:25052-25058, 1992.
15. 15. Schleuning WD, Fritz H. Sperm acrosin. In Methods in Enzymology. New York: Academic Press, 1976, Vol. 43, pp 330-342.
16. 16. Byler DM, Susi H. Examination of the secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers 25:469-487, 1986.
17. 17. Surewicz WK, Mantsch HH. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim Biophys Acta 952:115-130, 1988.
18. 18. Surewicz WK, Mantsch HH, Chapman D. Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment Biochemistry 32:389-394, 1993.
19. 19. Casal HL, Kohler U, Mantsch HH. Structural and conformational changes of β-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature. Biochim Biophys Acta 957:11-20, 1988.
20. 20. Arrondo JLR, Muga A, Castresana J, Goni FM. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog Biophys Mol Biol 59:23-56, 1993.
21. 21. Krimm S, Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides and proteins. Adv Protein Chem 38:181-364, 1986.
22. 22. Muga A, Cistola DP, Mantsch HH. A comparative study of the conformational properties of Escherichia coli-derived rat intestinal and liver fatty acid binding proteins. Biochim Biophys Acta 1162:291-296, 1993.
23. 23. Chirgadze YN, Fedorow OW, Trushina NP. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers 14:679-694, 1975.
24. 24. Jackson M, Mantsch HH. Beware of proreins in DMSO. Biochim Biophys Acta 1078:231-235, 1991.
25. 25. Jackson M, Mantsch HH. Halogenated alcohols as solvents for proteins: FTIR spectroscopic studies. Biochim Biophys Acta 1118:139-143, 1992.
26. 26. Fernandez-Ballester G, Castresana J, Arrondo JLR, Ferragut JA, Gonzales-Ros JM. Protein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopy. Biochem J 288:421-426, 1992.
27. 27. Jones R. Unusual fucoidan-binding properties of chymotrypsinogen and trypsinogen. Biochim Biophys Acta 1037:227-232, 1990.
28. 28. Williams RM, Jones R. Specificity of binding of zona pellucida glycoproteins to sperm proacrosin and related proteins. J Exp Zool 266:65-73, 1993.
29. 29. Evans DLL, Christey PB, Carrel RW. The heparin binding site and activation of protease nexin I. In Serine Proteases and Their Serpin Inhibitors in the Nervous System (Festoff BW, Ed.). New York: Plenum, 1990, pp 69-78.
30. 30. Coffey RJ Jr, Leof EB, Shipley GD, Moses HL. Suramin inhibition of growth factor receptor binding and mitogenecity in AKR-2B cells. J Cell Physiol 132:143-148, 1987.
31. 31. Middaugh CR, Mach H, Burke CJ, Volkin DB, Dabora JM, Tsai PK, Bruner MW, Ryan JA, Marfia KE. Nature of the interaction of growth factors with suramin. Biochemistry 31:9016-9024, 1992.
32. 32. Yanagimachi R. Mammalian fertilization. In The Physiology of Reproduction (Knobil E, Neill JD, Eds). New York: Raven Press, 1994, pp 189-317.