IDENTIFICATION OF UNUSUAL REPLACEMENT OF METHIONINE BY NORLEUCINE IN RECOMBINANT INTERLEUKIN-2 PRODUCED BY ESCHERICHIA-COLI
IDENTIFICATION OF UNUSUAL REPLACEMENT OF METHIONINE BY NORLEUCINE IN RECOMBINANT INTERLEUKIN-2 PRODUCED BY ESCHERICHIA-COLI
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DOI：
10.1016/s0006-291x(88)80916-1
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发表时间：
1988-10-31
影响因子：
3.1
通讯作者：
LAI, PH
中科院分区：
文献类型：
--
作者：
LU, HS;TSAI, LB;LAI, PH
中等量的正亮氨酸掺入大肠杆菌产生的重组白细胞介素 2 (IL-2) 中。已检测到大肠杆菌。正亮氨酸的掺入发生在氨基末端和内部甲硫氨酸处，这通过含有正亮氨酸的胰蛋白酶肽的分离得到证实，该肽比各自的含有甲硫氨酸的肽通过反相HPLC洗脱得晚。通过氨基酸分析和氨基酸测序（包括埃德曼降解和快原子轰击质谱法）确定完整蛋白质和修饰肽中正亮氨酸的出现。在随后的论文中，我们确定正亮氨酸掺入是由大肠杆菌内源合成正亮氨酸引起的。大肠杆菌。
Moderate amounts of norleucine incorporation into recombinant interleukin-2 (IL-2) produced inE. colihave been detected. Incorporation of norleucine occurs both at the amino terminal and internal methionines as confirmed by the isolation of norleucine-containing tryptic peptides which eluted later than the respective methionine-containing peptides by reverse-phase HPLC. The occurence of norleucine in intact protein and modified peptides was determined by amino acid analysis and amino acid sequencing including Edman degradation and fast atom bombardment mass spectrometry. In the subsequent paper, we determined that norleucine incorporation is caused by the endogenous synthesis of norleucine inE. coli.