Department of Botany, University of Missouri, Columbia, Missouri 65201.
Plant Physiol. 1969 Feb;44(2):168-72. doi: 10.1104/pp.44.2.168.
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 (14)C 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.
采用圆盘电泳法将抗冻、不抗冻和受冻致死的甘蓝（甘蓝型油菜变种）叶片中的水溶性蛋白质进行分离。尽管个别蛋白带中的蛋白质含量发生了变化，但硬化后并没有发现任何新的条带出现，因为氨黑染色失败。用 2,2-二羟基-6,6-二萘基二硫化物对蛋白条带中的巯基进行染色，并标记为 (14)C p-氯汞苯甲酸。在硬化过程中和受冻致死过程中，总水溶性蛋白质中的巯基含量显著下降。在硬化过程中，水溶性蛋白质的显著增加与巯基含量的下降相吻合。由于受冻致死，每单位高分子量蛋白质的巯基含量显著增加，但总蛋白质的巯基含量却下降。这被解释为在冷冻过程中形成分子间二硫键的证据。
