Werle B, Ebert W, Klein W, Spiess E
Thoraxklinik Heidelberg; Germany.
Anticancer Res. 1996 Jan-Feb;16(1):49-53.
Secreted pro-cathepsin B of HS-24 human lung-tumour cells, human alveolar macrophages and Wi-38 human lung-fibroblast cells was pre-purified by ion exchange chromatography and investigated by 2D gel electrophoresis. Four (Wi-38), six (HS-24) and ten (alveolar macrophages) polypeptides differing in charge, but with the same molecular mass of 45 kDa, were found. The isoelectrical points of these polypeptides ranged from 5.43 to 6.57. Deglycosylation reduced the mass (7 kDa) but did not change the charge pattern. This investigation established cell type-specific patterns of secreted pro-cathepsin B-forms, but only parts of these may be cell type-specific forms depending on differentiated expression of mRNA and post-translational modification.
通过离子交换色谱法对HS-24人肺肿瘤细胞、人肺泡巨噬细胞和Wi-38人肺成纤维细胞分泌的组织蛋白酶B前体进行预纯化，并通过二维凝胶电泳进行研究。发现了电荷不同但分子量均为45 kDa的四种（Wi-38）、六种（HS-24）和十种（肺泡巨噬细胞）多肽。这些多肽的等电点范围为5.43至6.57。去糖基化降低了质量（7 kDa），但没有改变电荷模式。这项研究确定了分泌的组织蛋白酶B前体形式的细胞类型特异性模式，但其中只有部分可能是取决于mRNA的分化表达和翻译后修饰的细胞类型特异性形式。
