Abstract
The decapacitating fraction of human seminal plasma, which strongly interacts with concanavalin A, is constituted by high mannose–type N-linked glycoproteins, most of them of less than 44 kDa. Each component with apparent molecular mass of 30, 18, and 17 kDa respectively, as judged by SDS-PAGE, was submitted to “in gel” digestion with trypsin followed by HPLC separation of the peptides and sequencing. They were characterized at microscale as gp17, an aspartyl protease that possibly contributes to liquefaction of the seminal plasma coagulum, two fragments of human acid phosphatase (17 and 30 kDa, respectively), and a 17-kDa fragment of carboxypeptidase E. Neither the fragments of prostatic acid phosphatase nor that of carboxypeptidase E had been described before in the human seminal fluid. Very weak bands, of apparent molecular masses 44 and 52 kDa, are consistent with presence of small amounts of parent compounds, prostatic acid phosphatase and carboxypeptidase E.
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REFERENCES
Autiero, M., Gaubin, M., Mani, J. C., Castejón, C., Martín, M., Marthorny, S., Guardiola, J., and Piatier-Tonneau, D. (1997). Eur. J. Biochem. 245: 208–213.
Basmaciogullari, S., Autiero, M., Culerrier, R., Mani, J. C., Gaubin, M., Mishal, Z., Guardiola, J., Granier, C., and Piatier-Tonneau, D. (2000). Biochemistry 39: 5332–5340.
Benoff, S. (1997). Mol. Hum. Reprod. 7: 599–637.
Brillard-Bourdet, M., Réhault, S., Juliano, L., Ferrer, M., Moreau, T., and Gauthier, F. (2002). Eur. J. Biochem. 269: 390–395.
Calvete, J. J., Varela, P. F., Sanz, L., Romero, A., Mann, K., and Topfer-Petersen, E. (1996). Prot. Exp. Purif. 8: 48–56.
Caputo, E., Autiero, M., Mani, J. C., Basmaciogullari, S., Pintier-Tonneau, D., and Guardiola, J. (1998). Int. J. Cancer 78: 76–85.
Caputo, E., Manco, G., Mandrich, L., and Guardiola, J. (2000). J. Biol. Chem. 275: 7935–7941.
Carlsson, S. R. (1993). In Glycobiology. A practical approach (Fukuda, M., and Kobata, A., eds.), IRL Press, Oxford University Press, Oxford, New York, Tokyo. pp. 15–16.
D'Cruz, O. J., Lambert, H., and Haas, G. G., Jr. (1997). Am. J. Reprod. Immunol. 37: 172–183.
Drisdel, R. C., Mack, S. R., Anderson, R. A., and Zaneveld, L. J. D. (1995). Biol. Reprod. 53: 201–208.
Dubois, M., Gilles, K. A., Robers, P. A., and Smith, F. (1956). Anal. Chem. 28: 350–356.
Iborra, A., Morte, C., Fuente, P., García-Framis, V., Andolz, P., and Martinez, P. (1996). Am. J. Reprod. Immunol. 36: 118–125.
Killian, G. L., Chapman, D. A., and Rogowski, L. A. (1993). Biol. Reprod. 49: 1202–1207.
Kobata, E., and Yamashita, K. (1993). In Glycobiology. A practical approach (Fukuda, M., and Kobata, A., eds.), IRL Press, Oxford University Press, Oxford, New York, Tokyo, p. 110.
Laemmli, K. (1970). Nat. (Lond.) 277: 680–685.
Lelli, S., Marquínez, A. C., Merani, M. S., and Scacciati de Cerezo, J. M. (1994). Glycobiology 4: 94.
Lelli, S., and Scacciati de Cerezo, J. M. (1999). Isol. Purif. 3: 21–27.
Lin, M. F., Lee, M. S., Zhou, X. W., Andressen, J. C., Meng, T. C., Johansson, S. L., West, W. W., Taylor, R. J., Anderson, J. R., and Lin, F. F. (2001). J. Urol. 166: 1943–1950.
Loeser, C. R., and Tulsiani, D. R. P. (1999). Biol. Reprod. 60: 94–101.
Lowry, O. H., Rosenbrough, N. J., Farr, A. L., and Randall, R. J. (1951). J. Biol. Chem. 193: 265–275.
Manser, E., Fernandez, D., Loo, L., Goh, P. Y., Monfries, C., Hall, C., and Lim, L. (1990). Biochem. J. 267: 517–525.
Marquínez, A. C., Andreetta, A. M., Chen, J. S., Menesini Chen, M. G., Wolfenstein-Todel, C., and Scacciati de Cerezo, J. M. (2000). J. Chromatogr. B. 746: 141–150.
Mazzini, M. N., Cerezo, A. S., and Scacciati de Cerezo, J. M. (1979). J. Chromatogr. 173: 365–371.
Ostrowski, W. S., and Kuciel, R. (1994). Clin. Chim. Acta 226: 121–129.
Rosenfeld, J., Capdeville, J., Guillemont, J. C., and Ferrara, P. (1992). Anal. Biochem. 203: 173–179.
Scacciati de Cerezo, J. M., Marquínez, A. C., Sarchi, M. I., and Cerezo, A. S. (1996). Biocell 20: 11–19.
Sharief, F. S., Lee, H., Leuderman, M. M., Lundwall, A., Deaven, L. L., Lee, C., and Li, S. S. (1989). Biochem. Biophys. Res. Commun. 160: 79–86.
Starita-Geribaldi, M., Poggioli, S., Zucchini, M., Garin, J., Chevallier, D., Fenichel, P., and Pointis, G. (2001). Mol. Hum. Reprod. 7: 715–722.
Takayama, T. K., McMullen, B. A., Nelson, P. S., Matsumura, M., and Fujikawa, K. (2001). Biochemistry 40: 15341–15348.
Thérien, I., Bleau, G., and Manjunath, P. (1995). Biol. Reprod. 52: 1372–1379.
Tortorella, H., Scacciati de Cerezo, J. M., Mazzini, M. N., and Cerezo, A. S. (1983). Am. J. Reprod. Immunol. 4: 76–82.
Warren, L. (1959) J. Biol. Chem. 234: 1971–1975.
WHO laboratory manual for examination of human semen and sperm cervical mucus interaction (1992) University of Cambridge, Cambridge, U.K.
Yamamoto, K., Tsuji, T., and Osawa, T. (1993). In: Methods in molecular biology (E. F. Hounsell, ed.), Humana Press, Totowa, NJ, vol 14, pp. 26–27.
Yonesawa, N., Aoki, H., Hatanaka, Y., and Nakano, M. (1995). Eur. J. Biochem. (FEBS) 233: 35–41.
Yonesawa, N., Mitsui, S., Kudo, K., and Nakano, M. (1997). Eur. J. Biochem. (FEBS) 248: 86–92.
Zdebska, E., and Kóscielak, J. (1999). Anal. Biochem. 275: 171–179.
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Marquínez, A.C., Andreetta, A.M., González, N. et al. Identification of gp17 Glycoprotein and Characterization of Prostatic Acid Phosphatase (PAP) and Carboxypeptidase E (CPE) Fragments in a Human Seminal Plasma Fraction Interacting with Concanavalin A. J Protein Chem 22, 423–429 (2003). https://doi.org/10.1023/B:JOPC.0000005457.29475.d7
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DOI: https://doi.org/10.1023/B:JOPC.0000005457.29475.d7