Processing of enkephalin precursors by chromaffin granule enzymes.
Processing of enkephalin precursors by chromaffin granule enzymes.
复制标题
通过嗜铬颗粒酶加工脑啡肽前体。
DOI：
10.1016/0024-3205(82)90193-x
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发表时间：
1982
期刊：
影响因子：
6.1
通讯作者：
Musacchio,JM
中科院分区：
文献类型：
--
作者：
Troy,CM;Musacchio,JM
Subcellular localization studies indicate that the enzyme activities which cleave enkephalins from larger polypeptides are located in both membranous and soluble components of the chromaffin granules and not in the lysosomes. Cleavage of endogenous precursors produced methionine enkephalin [Met-E], leucine enkephalin [Leu-E], and Met-E-Arg6. Cleavage of synthetic peptide E produced Leu-E, Met-E, and Met-E-Arg6. The pH optimum for enkephalin production is pH 5.7. Dithiothreitol prevents the inhibition of enkephalin conversion produced by p-chloromecurobenzoate. Studies with peptide E indicate that cleavage appears to occur at apairs of basic amino acid residues. The presence of enkephalin producing enzymes with the precursors and the products in the chromaffin granules could be important in the elucidation of the factors that regulate enkephalin biosynthesis.
