Proteolytic enzymes from the mouse submaxillary gland. Specificity restricted to arginine residues.
Proteolytic enzymes from the mouse submaxillary gland. Specificity restricted to arginine residues.
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来自小鼠颌下腺的蛋白水解酶。
DOI：
10.1016/0003-9861(77)90283-1
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发表时间：
1977
影响因子：
3.9
通讯作者：
B. Frangione
中科院分区：
文献类型：
--
作者：
I. Schenkein;M. Levy;E. Franklin;B. Frangione
小鼠颌下蛋白酶（A + D），其分离和性质已由我们先前描述，仅水解蛋白质中的乙酰基键。聚精氨酸、聚赖氨酸、溶菌酶、组蛋白和胰岛素的底物的甲醛滴定和肽图谱表明了这种特异性。从溶菌酶和胰岛素的肽的氨基酸组成表明，大多数但不是所有的乙酰基键水解，但没有赖氨酰键分裂。这些蛋白酶在蛋白质的测序中应该是有用的。
The mouse submaxillary proteases (A + D), the isolation and properties of which were previously described by us, hydrolyze only arginyl bonds in proteins. Formol titrations and peptide mapping on digests of polyarginine, polylysine, lysozyme, histone, and insulin suggested this specificity. Amino acid compositions of peptides from lysozyme and insulin showed that most but not all arginyl bonds were hydrolyzed but that no lysyl bonds were split. The proteases should be useful in the sequencing of proteins.