Abstract
The denaturation of protein by pressure has been generally well known since the findings of the perfect coagulation of egg white by a pressure of 7,000 atm within 30 min by Bridgman (J Biol Chem 19:511–512, 1914), and Kiyama and Yanagimoto (Rev Phys Chem Jpn 21:41–43, 1951) confirmed that the coagulation occurs above 3,880 kg cm−2. Grant et al. (Science 94:616, 1941) and Suzuki and Kitamura (Abstracts of 30th annual meeting of Japanese Biochemical Society, 1957) found that SH groups are detected at the compressed sample of ovalbumin. On the other hand, Johnson and Campbell (J Cell Comp Physiol 26:43–49, 1945), Tongur (Kolloid Zhur 11:274–279, 1949; Biokhimiya 17:495–503, 1952) and Suzuki et al. (Mem Res Inst Sci Eng Ritsumeikan Univ 3:1–4, 1958) reported that the thermal denaturation of proteins is retarded in a few examples by the low pressure of about 1,000 atm. Before 1960, the studies of denaturation under high pressure were, however, rare and almost qualitative compared with those by heat, acid, urea and so on, so that there was no theory for the influence of hydrostatic pressure on the mechanism of denaturation. Here I review how I started experiments and analysis on pressure denaturation of proteins in early days of 1950s and 1960s in my laboratory and others.
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Notes
- 1.
It was found from the experimental results of self-diffusion in water at 25 °C that the tetrahedrally coordinated structure of the usual water is broken down with the increase of pressure, and a stabilized new structure is formed around 4,000 atm. It was very interesting to note that the pressure denaturation begins at the same pressure region (Cuddeback et al. 1953).
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Suzuki, K. (2015). Early Days of Pressure Denaturation Studies of Proteins. In: Akasaka, K., Matsuki, H. (eds) High Pressure Bioscience. Subcellular Biochemistry, vol 72. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-9918-8_1
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