分析化学
分析化學
분석화학
CHINESE JOURNAL OF ANALYTICAL CHEMISTRY
2001年
2期
125-127
,共3页
王红霞%张学敏%杨松成%裴武红%李松
王紅霞%張學敏%楊鬆成%裴武紅%李鬆
왕홍하%장학민%양송성%배무홍%리송
FK结合蛋白12%基体辅助激光解析电离飞行时间质谱%肽质量指纹谱
FK結閤蛋白12%基體輔助激光解析電離飛行時間質譜%肽質量指紋譜
FK결합단백12%기체보조격광해석전리비행시간질보%태질량지문보
用MALDI-TOF-MS测定了具有生物活性的重组人 FK506结合蛋白12(rhFKP12)的分子量和胰蛋白酶酶解的肽质量指纹谱,实验测定结果与理论计算值一致。证明其一级结构是正确的,在表达、复性和纯化过程中没有氨基酸的丢失、变异和修饰。
用MALDI-TOF-MS測定瞭具有生物活性的重組人 FK506結閤蛋白12(rhFKP12)的分子量和胰蛋白酶酶解的肽質量指紋譜,實驗測定結果與理論計算值一緻。證明其一級結構是正確的,在錶達、複性和純化過程中沒有氨基痠的丟失、變異和脩飾。
용MALDI-TOF-MS측정료구유생물활성적중조인 FK506결합단백12(rhFKP12)적분자량화이단백매매해적태질량지문보,실험측정결과여이론계산치일치。증명기일급결구시정학적,재표체、복성화순화과정중몰유안기산적주실、변이화수식。
The primary structure of rhFK506-Binding Protein (FKBP) 12 was studied with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) by measuring its molecular weight and tryptic peptide mass fingerprinting.The calculated molecular weight of rhFKBP12 was 11819.5 and the measured value was 11818.0. The relative error was only 0.01%. The measured peptide mass fingrprinting of rhFKBP12was identical with that deduced from its amino acid sequence. It proved that the primary structure of rhFKBP12 was correct and there was no amino acid deletion, mutation and modification in its expression, refolding andpurification.