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. 2004 May;135(1):364–376. doi: 10.1104/pp.103.038158

Table I.

Effect of cations and freeze-thaw cycles on the structure of apoplastic proteins from winter rye leaves as determined by Trp fluorescence

Salt No. of Freeze-Thaw Cycles λmax
nm
EDTA 0 327.7 ± 0.3, 360.3 ± 0.3
EDTA 3 355.2 ± 0.2
CaCl2 0 336.5 ± 0.2
CaCl2 3 335.5 ± 0.0
MgCl2 0 336.3 ± 0.2
MgCl2 3 334.8 ± 0.4

Proteins were dialyzed in 5 mm EDTA, 20 mm CaCl2, or 20 mm MgCl2. Half the samples were stored at 4°C until analysis as unfrozen controls, and the remaining samples were subjected to three freeze-thaw cycles in which they were frozen at −20°C for 2 h and thawed at 20°C for 5 min. Trp residues were excited at 280 nm, and the wavelengths of maximum fluorescence emission (λmax) were recorded. Data are presented as means ±se, n = 3.