Ca2+-binding and protein-protein interaction domains of the sea urchin extraembryonic coat protein hyalin |
| |
Institution: | 1. Energy Environment Policy and Technology, Graduate School of Energy and Environment (KU-KIST Green School), Korea University, 145 Anam-ro, Sungbuk-gu, Seoul, South Korea;2. Department of Integrative Energy Engineering, College of Engineering, Korea University, 145 Anam-ro, Sungbuk-gu, Seoul 02841, South Korea;3. Policy Department, Korea Institute of Science and Technology, 5 Hwarang-ro 14-gil, Sungbuk-gu, Seoul 02792, South Korea |
| |
Abstract: | - 1.1. As reported previously (Hopper and Robinson, 1990; Int. J. Biochem. 22, 1165–1170) the sea urchin extraembryonic coat protein hyalin undergoes a Ca2+-induced self-association into an insoluble gel (gelation) in the presence of Mg2+ and/or NaCl.
- 2.2. A 275 kDa peptide fragment, generated by limited tryptic digestion of hyalin, binds Ca2++ but does not undergo gelation in the presence of Ca2+, Mg2+ and NaCl.
- 3.3. Comparisons between the capacities of hyalin and the 275 kDa peptide fragment to bind Ca2+ indicate that the latter binds 88% less Ca2+ than hyalin.
- 4.4. However, the presence of Ca2+ alone, at a concentration of 5 mM, protects the 275 kDa peptide fragment from further digestion by trypsin mimicking the effect of this cation in protecting hyalin.
- 5.5. Gel exclusion Chromatographie analyses of the 275 kDa peptide fragment, both in the presence and absence of 5 mM Ca2+, indicate that this cation does induce self-association of the fragment.
- 6.6. These results provide information on the organization of the functional domains on hyalin which are required for gel formation.
|
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |
|