Turbidimetric studies of Limulus coagulin gel formation

Biophysical Journal

Volumn 71, Issue 4, 1996, Pages 2012-2021

  Moody, Thomas P ^a   Donovan, Maribeth A ^b   Laue, Thomas M ^a  

^a UNIVERSITY OF NEW HAMPSHIRE   (United States)

^b Biotechnology Division   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COAGULIN; PROTEIN; TRYPSIN; UNCLASSIFIED DRUG;

ARTICLE; BLOOD CLOTTING; CRAB; LIGHT ABSORPTION; LIMULUS; MOLECULAR MODEL; NONHUMAN; PROTEIN ANALYSIS; SPECTRAL SENSITIVITY; STRUCTURE ANALYSIS; TURBIDIMETRY;

DECAPODA (CRUSTACEA); LIMULUS;

EID: 0029820370     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79399-2     Document Type: Article

References (45)

1. Andreu, J., and S. N. Timasheff. 1986. The measurement of cooperative protein self-assembly by turbidity and other techniques. Methods Enzymol 130:47-59.
2. Bang, F. B. 1956. A bacterial disease of Limulus polyphemus. Bull. Johns Hopkins Hosp. 98:325-337.
3. Berkowitz, S. A., and L. A. Day. 1980. Turbidity measurements in an analytical ultracentrifuge. Determinations of mass per length for filamentous viruses fd, Xf, and Pf3. Biochemistry. 19:2696-2702.
4. Camerini-Otero, R. D., and L. A. Day. 1978. The wavelength dependence of the turbidity of solutions of macromolecules. Biopolymers. 17:2241-2249.
5. Camerini-Otero, R. D., R. M. Franklin, and L. A. Day. 1974. Molecular weights, dispersion of refractive index increments, and dimensions from transmittance spectrophotometry. Bacteriophages R17, T7, and PM2, and tobacco mosaic virus. Biochemistry. 13:3763-3773.
6. Cancellieri, A., C. Frontali, and E. Gratton. 1974. Dispersion effect on turbidimetric size measurement. Biopolymers. 13:735-743.
7. Cantor, C. R., and P. R. Schimmel. 1980. Other scattering and diffraction techniques. In Biophysical Chemistry. Part II: Techniques for the Study of Biological Structure and Function. W. H. Freeman and Co., San Francisco. 838-846.
8. Casassa, E. F., and H. Eisenberg. 1964. Thermodynamic analysis of multicomponent solutions. Adv. Protein Chem. 19:287-395.
9. Castellan, G. W. 1983. Polymers. In Physical Chemistry. Addison-Wesley Publishing Co., Reading, MA. 929-935.
10. Cheng, S. M., A. Suzuki, G. Zon, and T. Y. Liu. 1986. Characterization of a complementary deoxyribonucleic acid for the coagulogen of Limulus polyphemus. Biochim. Biophys. Acta. 868:1-8.
11. Chou, R. R., M. H. Stromer, R. M. Robson, and T. W. Huialt. 1990. Determination of the critical concentration required for desmin assembly. Biochem. J. 272:139-145.
12. Debye, P. 1954. Angular dissymmetry of scattering and shape of particles. In The Collected Papers of Peter J. W. Debye. Interscience, New York. 500-513.
13. De Cristofaro, R., and E. Di Cera. 1991. Phenomenological analysis of the clotting curve. J. Protein Chem. 10:455-468.
14. Donovan, M. A. 1990. Initial characterization of coagulogen polymerization and a novel trypsin inhibitor from Limulus polyphemus. Ph.D. dissertation. University of New Hampshire, Durham, NH.
15. Donovan, M. A., and T. M. Laue. 1991. A novel trypsin inhibitor from the horseshoe crab Limulus polyphemus. J. Biol. Chem. 266:2121-2125.
16. Doty, P., And R. F. Steiner. 1950. Light scattering and spectrophotometry of colloidal solutions. J. Chem. Phys. 18:1211-1220.
17. Feynman, R. P. 1965. Reflection from surfaces. In The Feynman Lectures on Physics, Vol. 2. R. P. Feynman, R. B. Leighton, and M. Sands, editors. Addison Wesley Publishing Co., Reading, MA. 33.
18. Gaffin, S. L. 1976. The clotting of the lysed white cells of Limulus induced by endotoxin. I. Preparation and characterization of clot-forming proteins. Biorheology. 13:237-280.
19. Gaskin, F., C. Cantor, M. Shelanski, and B. Berne. 1974. Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules. J. Mol. Biol. 89:737-758.
20. Geiduschek, E. P., and A. Holtzer. 1958. Application of light scattering to biological systems: deoxyribonucleic acid and the muscle proteins. Adv. Biol. Med. Phys. 6:431-551.
21. Hantgan, R. R., and J. Hermans. 1979. Assembly of fibrin: a light scattering study. J. Biol. Chem. 254:11272-11281.
22. Hantgan, R., J. McDonagh, and J. Hermans. 1983. Fibrin assembly. Ann. N.Y. Acad. Sci. 408:344-366.
23. Holme, R., and N. O. Solum. 1973. Electron microscopy of the gel protein formed by clotting of Limulus polyphemus hemocyte extracts. J. Ultrastruct. Res. 44:329-338.
24. Johnson, K. A., and G. G. Borisy. 1979. Thermodynamic analysis of microtubule self-assembly in vitro. J. Mol. Biol. 133:199-216.
25. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
26. Liu, T., R. C. Seid, J. Tai, S. Liang, T. P. Sakmar, and J. B. Robbins. 1979. Studies on Limulus lysate coagulating system. In Biomedical Applications of the Horseshoe Crab (Limulidae). E. Cohen, editor. Alan R. Liss, New York. 147-158.
27. Miyata, T., M. Hiranaga, M. Umezu, and S. Iwanaga. 1983. The complete amino acid sequence of coagulogen isolated from Limulus polyphemus amebocytes. Ann. N.Y. Acad. Sci. 408:651-654.
28. Miyata, T., M. Hiranaga, M. Umezu, and I. Sadaaki. 1984. Amino acid sequence of the coagulogen from Limulus polyphemus hemocytes. J. Biol. Chem. 259:8924-8933.
29. Moody, T. P. 1994. Physical studies of Limulus coagulogen, the coagulin gel and coagulin gel formation. Ph.D, dissertation. University of New Hampshire, Durham, NH.
30. Nakamura, S., S. Iwanaga, T. Harada, and M. Niwa. 1976. A clottable protein (coagulogen) from amoebocyte lysate of Japanese horseshoe crab (Tachypleus tridentatus). J. Biochem. 80:1011-1021.
31. Oosawa, F., and S. Asakura. 1975. Energetics. In Thermodynamics of the Polymerization of Protein. Academic Press, London. 56-69.
32. Rawn, J. D. 1983. Enzyme kinetics. In Biochemistry. Harper and Row, New York. 225-267.
33. Shishikura, F., S. Nakamura, K. Takahashi, and K. Sekiguchi. 1982. Horseshoe crab phylogeny based on amino acid sequences of the fibrinopeptide-like peptide C. J. Exp. Zool. 223:89-91.
34. Shishikura, F., S. Nakamura, K. Takahashi, and K. Sekiguchi. 1983. Coagulogens from four living species of horseshoe crab (Limulidae): comparison of their biochemical and immunochemical properties. J. Biochem. 94:1279-1287.
35. Solum, N. O. 1970. Some characteristics of the clottable protein of Limulus polyphemus blood cells. Thromb. Diath. Haemorrh. 23:170-181.
36. Solum, N. O. 1973. The coagulogen of Limulus polyphemus hemocytes. A comparison of the clotted and non-clotted forms of the molecule. Thromb. Rex. 2:55-70.
37. Tai, J. T., R. C. Seid, Jr., R. D. Huhn, and T. Y. Liu. 1977. Studies on Limulus amoebocyte lysate. II. Purification of the coagulogen and the mechanism of clotting. J. Biol. Chem. 252:4773-4776.
38. Takagi, T., Y. Hokama, T. Morita, S. Iwanaga, S. Nakamura, and M. Niwa. 1979. Amino acid sequence studies on horseshoe crab (Tachypleus tridentatus) coagulogen and the mechanism of gel formation. In Biomedical Applications of the Horseshoe Crab (Limulidae). E. Cohen, editor. Alan R. Liss, New York. 169-184.
39. Tanford, C. 1961. Light scattering. In Physical Chemistry of Macromolecules. John Wiley and Sons, New York. 275-316.
40. Timasheff, S. N. 1981. The self-assembly of long rodlike structures. In Protein-Protein Interactions. C. Frieden and L. W. Nichol, editors. John Wiley and Sons, New York. 315-336.
41. van de Hulst, H. C. 1957. Introduction. In Light Scattering by Small Particles. John Wiley and Sons, New York. 3-10.
42. van Holde, K. E. 1985. Scattering. In Physical Biochemistry. Prentice-Hall, Englewood Cliffs, NJ. 203-234.
43. Weisel, J. W., C. Nagaswami, and L. Makowski. 1987. Twisting of fibrin fibers limits their radial growth. Proc. Natl. Acad. Sci. USA. 84: 8991-8995.
44. Zimm, B. H. 1948a. The scattering of light and the radial distribution function of high polymer solutions. J. Chem. Phys. 16:1093-1098.
45. Zimm, B. H. 1948b. Apparatus and methods for measurement and interpretation of the angular variation of light scattering: preliminary results on polystyrene solutions. J. Chem. Phys. 16:1099-1116.