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尿液糖蛋白(Tamm-Horsfanll 蛋白,简称 TH蛋白)首先由 Tamm 和 Horsfall 二人分离和描述。McQeen 检查一肾病患者透明管型,证明其中所含的 TH 蛋白量50倍于白蛋白,首先确认管型的基质主要是 TH 蛋白。最近资料指出此种蛋白可能与某些肾脏疾病的发病原因有关。TH 蛋白凝集分子量很大,可超过7×10~6dalton。电子显微镜下,溶于稀盐溶液中的 TH 蛋白为长短不一的细长丝,有一规律的弯曲不分支的螺旋状结构;在高浓度盐溶液中,这些细长丝似乎在侧侧之间相连成束。用解离剂可解离为分子量大约100,000dalton 的基团。人类、兔、田鼠的 TH 蛋白的氨基酸成分比例无明显差别。TH 蛋白中半胱氨酸残基含量比其他糖蛋白高得多。人类的每个 TH 蛋白分子
Urine glycoprotein (Tamm-Horsfanll protein, referred to as TH protein) was first isolated and described by two Tamm and Horsfall. McQeen examination of a kidney disease in patients with transparent tube proved that it contains 50 times the TH protein albumin, the first to confirm that the tubular matrix is mainly TH protein. Recent data indicate that this protein may be related to the pathogenesis of certain kidney diseases. TH protein aggregation molecular weight can be more than 7 × 10 ~ 6dalton. Under electron microscopy, the TH protein dissolved in dilute salt solution is an elongated filament of varying lengths and has a regular helical, unbranched spiral structure; these filaments appear to be laterally in high concentration saline Connected into bundles. Dissociation agents are used to dissociate groups having a molecular weight of about 100,000 daltons. There was no significant difference in the amino acid composition of TH protein in human, rabbit and vole. The TH protein contains much more cysteine residues than other glycoproteins. Every human TH protein molecule