Hostname: page-component-78c5997874-fbnjt Total loading time: 0 Render date: 2024-11-17T23:30:11.005Z Has data issue: false hasContentIssue false
  • English
  • Français

Is the Tyrosine Rich Eggshell Protein of Schistosoma Mansoni an Electron Transport Chain?

Published online by Cambridge University Press:  15 February 2011

John S. Cordingley ,
John A. Thomson  and
C. Russell Middaugh
John S. Cordingley
Affiliation:
Dept. of Molecular Biology, University of Wyoming, Box 3944 University Station, Laramie, WY 82071, U.S.A.
John A. Thomson
Affiliation:
Dept. of Molecular Biology, University of Wyoming, Box 3944 University Station, Laramie, WY 82071, U.S.A.
C. Russell Middaugh
Affiliation:
Dept. of Molecular Biology, University of Wyoming, Box 3944 University Station, Laramie, WY 82071, U.S.A.
Get access

Abstract

The schistosome eggshell is composed of two kinds of cross-linked proteins. One is glycine rich and the other is extremely tyrosine rich and highly repetitive. The highly conserved sequence of the tyrosine residues in the tyrosine rich protein suggests that it may play a role as an electron transport chain during eggshell cross-linking. Studies using model synthetic peptides suggest that the tyrosine rich protein may adopt a left-handed structure, possibly a left-handed alpha-helix.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 292: Symposium S – Biomolecular Materials , 1992 , 69
Copyright
Copyright © Materials Research Society 1993

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Wells, K.E. and Cordingley, J.S. (1991) Exp. Parasitol., 73, 295.Google Scholar
2. Wells, K.E. and Cordingley, J.S. (1992) in Case, S.T. (ed.), Structure, Cellular Synthesis and Assembly of Biopolymers. Springer-Verlag, New York, p.97.Google Scholar
3. Byram, J.E. and Senft, A.W. (1979) Am. J. Trop. Med. Hyg., 28, 539.Google Scholar
4. Seed, J.L. and Bennet, J.L. (1980) Exp. Parasitol., 49, 430.Google Scholar
5. Seed, J.L., Kilts, C.D. and Bennet, J.L. (1980) Exp. Parasitol., 50, 33.Google Scholar
6. Bobek, L.A., Rekosh, D.M. and Loverde, P.T. (1988) Molecular and Cellular Biology, 8, 3008.Google Scholar
7. Kunz, W., Opatz, K., Finken, M. and Symmons, P. (1987) Nucl. Acids Res., 15, 5894.Google Scholar
8. Johnson, K.S., Taylor, D.W. and Cordingley, J.S. (1987) Mol. Biochem. Parasitol., 22, 89.Google Scholar
9. Chen, L., Rekosh, D.M. and Loverde, P.T. (1992) Mol. Biochem. Parasitol., 52, 39.Google Scholar
10. Shibahara, S., Tomita, Y., Sakakura, T., Nager, C., Chaudhuri, B. and Muller, R. (1986) Nucl. Acids Res., 14, 2413.Google Scholar
11. Meadows, H.M. and Simpson, A.J.G. (1989) Mol. Biochem. Parasitol., 36, 291.Google Scholar
12. Metz, J.G., Nixon, P.J., Rogner, M., Brudvig, G.W. and Diner, B.A. (1989) Biochemistry, 28, 6960.Google Scholar