| Autor: |
Seiichi Era, Masaru Sogami, Kazuo Kuwata, Shunji Nagaoka, Kiyoshi Shiga, Kazuyuki Akasaka, Hiroshi Watari, Kimihiro Kida, Hiroshi Inouye |
| Rok vydání: |
2009 |
| Předmět: |
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| Zdroj: |
International Journal of Peptide and Protein Research. 28:130-140 |
| ISSN: |
0367-8377 |
| DOI: |
10.1111/j.1399-3011.1986.tb03239.x |
| Popis: |
Bovine plasma albumin Fr. V (BPA) has been known to contain small amounts of proteolytic enzyme. Wilson & Foster (1971) found a very limited and specific cleavage of BPA catalyzed by the enzyme with BPA in the F-form near pH 3.8, resulting in the formation of partially hydrolyzed BPA (BPA*). BPA* had a tendency to form a transparent gel at pD 4.0 (pD range of the F-form) above 8%, though proteolytic enzyme-free bovine mercaptalbumin (BMA) was in a transparent solution at pD 4.0 even at 12%. Water structures of the F-form of BMA in the solution state and of BPA* in the gel state were studied by measuring 1H-n.m.r. spectra, spin-lattice relaxation time (T1) and cross relaxation time (TIS) between irradiated and observed protons. Protein concentration-dependent changes of T1 of water protons indicated that the amount of hydrated water of BPA* in the gel state is far greater than that of the F-form of BMA in the solution state. TIS values from protein protons to water protons also indicated a large amount of hydration of BPA*, strong interaction between water and BPA* and rapid exchange between bound and bulk water in the gel state. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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