A Physicochemical Basis for the Selection of Osmolytes by Nature
It is a striking fact of nature that compounds used as cellular osmolyte systems by a variety of plant and animal vertebrate and invertebrate systems are confined to a small number of chemical structures, all, or most of which are distributed over the entire gamut of organisms (Yancey et al. 1982; Somero 1986; Somero, this Vol.). These comprise sugars and other polyols, amino acids and amino acid derivatives, methylamines, and in some cases urea, frequently in combination with methylamines All are electrically neutral molecules. With the exception of urea all of these organic osmolytes are “compatible solutes” (Brown and Simpson 1972; Clark 1985), i.e., they do not disturb cellular structure and function. Among amino acids, arginine and lysine are not used as osmolytes (Yancey et al. 1982). They are known to be “incompatible” (Somero 1986), in that they interfere with some biochemical processes. Nor are amino acids that contain large hydrophobic side chains used. It is noteworthy that in a case where arginine is released it is immediately converted to the “compatible” solute octopine (Hochachka et al. 1977).
KeywordsOsmotic Pressure Glycine Betaine Denature State Preferential Interaction Peptide Group
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- Cohn EJ, Edsall JT (1943) Proteins, amino acids and peptides. Reinhold, New York, p 218Google Scholar
- Gekko K, Morikawa T (1981) Preferential hydration of bovine serum albumin in polyhydric alcohol-water mixtures. J Biochem Jpn 90: 39–50Google Scholar
- Gibbs JW (1878) On the equilibrium of heterogeneous substances. Trans Conn Acad 3: 343–524Google Scholar
- Landt E (1931) The surface tensions of solutions of various sugars. Z Ver Dtsch Zuckerind 81: 119–124Google Scholar
- Morse HN, Holland WW, Myers CN, Cash G, Zinn JB (1912) The omostic pressure of cane sugar solutions at high temperature. In: Washburn EW (ed) International Critical Tables (1928) 4:429. Am Chem J 48: 29–94Google Scholar
- Smith PK, Smith ERB (1937) The activity of aliphatic amino acids in aqueous solution at 25 °C. J Biol Chem 121: 607–613Google Scholar
- Smith PK, Smith ERB (1940) The activities of some hydroxy-and N-methylamino acids and proline in aqueous solution at 25 °C. J Biol Chem 132: 57–64Google Scholar
- Tanford C (1973) The hydrophobic effect: formation of micelles and biological membranes. Wiley, New York LondonGoogle Scholar
- Timasheff SN (1991) Stabilization of protein structure by solvent additives. In: Ahern TJ, Manning M (eds) Stability of protein pharmaceuticals: in vivo pathways of degradation and strategies for protein stabilization, Vol 3Google Scholar
- von Hippel PH, Wong K-Y (1965) On the conformational stability of globular proteins. J Biol Chem 240: 3909–3923Google Scholar
- von Hippel PH, Wong K-Y (1965) On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition. J Biol Chem 240: 3909–3923Google Scholar
- Wyn-Jones RG, Storey R, Leigh RA, Ahmad N, Pollard A (1977) A hypothesis on cytoplasmic osmoregulation. In: Marre E, Cifferi O (eds) Regulation of cell membrane activities in plants. North Holland, Amsterdam, p 121Google Scholar