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Familial amyloid polyneuropathy transthyretin damages the chemical modification
PAGE \* MERGEFORMAT 11
Familial amyloid polyneuropathy transthyretin damages the chemical modification
Authors: Zhao Hui, Jin-Ping Liu, Fang Zheng, Liu Xiaochun, Li Xin, Song Jia-Yin, Sun added the country
[Abstract] Objective: To establish an analysis of plasma lipoproteins that there Transthyretin (TTR) protein, chemical modification. Methods: Using PCR method of diagnosis of familial multiple nerve damage (FAP) in patients with gene mutation. Density gradient ultracentrifugation separation of normal, healthy and plasma lipoproteins in patients with FAP. the use of crystal vibration affinity between the sub-molecular device, analysis of TTR protein and lipoprotein affinity between the molecules. ELISA method of determination of plasma lipoprotein concentrations of TTR. using MALDI TOF MS Comparison of plasma and lipoprotein containing TTR protein level of chemical modification. Results: PCR method of diagnosis of FAP patients with TTR gene mutation. Analysis of normal human serum TTR and lipoprotein have affinity; normal human plasma lipoprotein TTR protein containing the TTR concentration and no significant difference between the FAP patients. FAP ATTR Val30Met patients with heterozygous TTR in plasma and lipoproteins containing proteins, the molecular weight protein found in four major TTR peaks. Conclusion: MALDI TOF MS method to analyze plasma, plasma lipoproteins containing TTR protein chemical modification.
[Keywords:] Lipoproteins; Transthyretin; nerve amyloid diseases, familial; chemical modification
[Abstract] AIM: To establish a method for analysis of transthyretin (TTR) modification in plasma. METHODS: TTR gene mutation was identified in familial amyloidotic polyneuropathy (FAP) patients using PCR and plasma lipoprotein was isolated from both FAP Val30Met patients and healthy volunteers using density gradient centrifugation. Affinity between TTR and plasma lipoprotein was analyzed by quartz crystal microbalance (QCM). Serum TTR l
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