Bålöw R M, Eriksson I
Biochem J. 1987 Jan 1;241(1):75-80. doi: 10.1042/bj2410075.
Rabbit antibodies against purified tripeptidyl peptidase II (TPP II) of human erythrocytes have been prepared and used in immunoblot analysis. Antibodies affinity-purified against the denatured 135,000-Mr subunit of the human peptidase were shown to cross-react with purified rat liver TPP II, as well as a polypeptide of Mr 135,000 in haemolysates and liver homogenates from several other species. TPP II activity in haemolysates from monkey, hog, horse and rabbit corresponded to the levels found in human erythrocytes, whereas this activity was absent or low in erythrocytes from calf and hen. On immunoblot analysis of the calf haemolysates, the 135,000-Mr polypeptide could not be detected. In contrast, analysis of liver homogenates from these species revealed both TPP activity and immunoreactive polypeptides. Immunoreactive polypeptides with Mr about 105,000 and 84,000 of variable occurrence were also detected. In addition, extracts of Escherichia coli showed no TPP II activity under the conditions of the standard assay, although polypeptides of Mr 135,000 and 40,000 were revealed on immunoblot analysis of this species.
已制备出针对人红细胞纯化的三肽基肽酶II（TPP II）的兔抗体，并将其用于免疫印迹分析。经证明，针对人肽酶变性的135,000道尔顿亚基亲和纯化的抗体，可与纯化的大鼠肝脏TPP II以及来自其他几个物种的溶血产物和肝脏匀浆中135,000道尔顿的多肽发生交叉反应。猴、猪、马和兔的溶血产物中的TPP II活性与人红细胞中的活性水平相当，而小牛和母鸡的红细胞中该活性缺失或较低。在对小牛溶血产物进行免疫印迹分析时，未检测到135,000道尔顿的多肽。相反，对这些物种的肝脏匀浆进行分析发现了TPP活性和免疫反应性多肽。还检测到了分子量约为105,000和84,000且出现情况各异的免疫反应性多肽。此外，在标准测定条件下，大肠杆菌提取物未显示出TPP II活性，尽管对该物种进行免疫印迹分析时发现了分子量为135,000和40,000的多肽。
