Narita H, Asaka Y, Ikura K, Matsumoto S, Sasaki R
Department of Food Science, Kyoto Women's University, Japan.
Eur J Biochem. 1995 Mar 15;228(3):855-62.
Three glycoproteins of 34, 38 and 40 kDa were isolated from the spent medium of suspension-cultured tobacco cells. The 38-kDa and 40-kDa proteins were highly cationic peroxidases with indistinguishable enzymic properties but their structural difference was confirmed by sequence analysis of the amino-terminal regions and the recognition specificity of monoclonal antibodies. The 34-kDa protein was a moderately cationic peroxidase with enzymic properties quite different from those of the 38-kDa and 40-kDa enzymes. They were undetectable in the spent medium during the cell-proliferation phase but became abundant in the medium during the cell-expansion phase. This was confirmed quantitatively with the 40-kDa protein using the 40-kDa-specific monoclonal antibody. The mRNA expression for 40-kDa protein was at a constant basal level in the cell-proliferation phase but increased in the cell-expansion phase.
从悬浮培养的烟草细胞的培养基中分离出了三种糖蛋白，分子量分别为34 kDa、38 kDa和40 kDa。38 kDa和40 kDa的蛋白质是高度阳离子化的过氧化物酶，酶学性质难以区分，但通过对氨基末端区域的序列分析和单克隆抗体的识别特异性证实了它们的结构差异。34 kDa的蛋白质是一种中度阳离子化的过氧化物酶，其酶学性质与38 kDa和40 kDa的酶有很大不同。在细胞增殖阶段，它们在培养基中无法检测到，但在细胞扩张阶段，它们在培养基中大量出现。使用40 kDa特异性单克隆抗体对40 kDa蛋白质进行了定量证实。40 kDa蛋白质的mRNA表达在细胞增殖阶段处于恒定的基础水平，但在细胞扩张阶段增加。
