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Effects of Freezing and Hardening on the Sulfhydryl Groups of Protein Fractions From Cabbage Leaves ¹

^a Department of Botany, University of Missouri, Columbia, Missouri 65201

Disc electrophoresis was used to separate water soluble proteins from hardy, non-hardy, and frost killed cabbage (Brassica oleracea var. capitata) leaves. Amidoschwarz staining failed to reveal any new bands as a result of hardening although the relative amounts of proteins in individual bands changed. Sulfhydryl groups in the protein bands were stained with 2,2-dihydroxy-6,6-dinaphthyl disulfide and labeled with ¹⁴C p-chloromercuribenzoate. Significant decreases in the sulfhydryl content of the total water soluble protein were found during hardening and as a result of frost death. The decrease during hardening was paralleled by a significant increase in the water soluble protein. There was a significant increase in the sulfhydryl content per unit high molecular weight protein but a decrease in the sulfhydryl content per total protein as a result of frost death. This was interpreted as evidence for intermolecular disulfide bond formation during freezing.

¹ Work supported in part by NSF grant NSF GB-4009, and NSF GB6828, and NIH Pre-Doctoral Fellowship No. 1-F1-Gm-32,208,01A1. Work done under the directorship of Dr. J. Levitt, Department of Botany, University of Missouri, Columbia, Missouri 65201 as part of the requirement for the degree of Ph.D.