Proteolytic enzymes from the mouse submaxillary gland: a partial sequence and demonstration of spontaneous cleavages.
Proteolytic enzymes from the mouse submaxillary gland: a partial sequence and demonstration of spontaneous cleavages.
复制标题
来自小鼠颌下腺的蛋白水解酶：自发裂解的部分序列和演示。
DOI：
10.1016/0003-9861(81)90256-3
复制
发表时间：
1981
影响因子：
3.9
通讯作者：
Frangione,B
中科院分区：
文献类型：
--
作者：
Schenkein,I;Franklin,EC;Frangione,B
小鼠上颌下蛋白酶（A和D），其分离和性质已经被我们描述过，只水解蛋白质中的精氨酸键。从氨基端确定了40个残基的序列。其结构与丝氨酸组的其他酶（如胰蛋白酶、凝血酶原、纤溶酶原、钾化酶）具有惊人的同源性（bbb50 %）。用二异丙基氟[32P]磷酸盐标记的单个肽的组成与上述蛋白酶的组成几乎相同，并且每个分子有一个活性位点被证实。这种酶很容易发生自发断裂，从而导致两次裂解。第一种是将A酶转化为D酶，同时损失一小段肽。第二种只能在还原后证明，因为碎片似乎是由二硫桥连接的。得到的两个分子量分别为14000和11000的片段是无活性的。
The mouse submaxillary proteases (A and D), whose isolation and properties were previously described by us, hydrolyze only arginyl bonds in proteins. The sequence of 40 residues from the amino terminus has been determined. Its structure shows a striking (>50%) homology with other enzymes of the serine group (e.g., trypsin, prothrombin, plasminogen, kallikrein). A single peptide labeled with diisopropylfluoro[32P]phosphate had a composition virtually identical to that found in the above proteases, and one active site per molecule was confirmed. The enzymes are very susceptible to spontaneous fragmentation which leads to two cleavages. The first converts enzyme A to D with loss of a small peptide. The second can only be demonstrated after reduction since the fragments appear to be joined by a disulfide bridge. The two resulting fragments with molecular weights of 14,000 and 11,000, respectively, are inactive.