Das Verhalten von TMV-Proteinmolekülen in verschiedenen Lösungsmitteln wurde untersucht. In Essigsäure liegen partiell denaturierte Monomere vom Mol.-Gew. 17 300 vor. In 0,01-n. NaOH bilden sich aus mehreren Monomeren stäbchenförmige Aggregate. In 36-proz. Harnstofflösung wird das TMV-Protein völlig denaturiert. Im Grenzfall unendlicher Verdünnung findet man isotrope monomere Fadenknäuel. Bei höherer Proteinkonzentration lagern sich diese in komplizierter Weise zu Aggregaten zusammen, die bei 2% Proteingehalt bereits aus durchschnittlich fünf Monomeren bestehen.
Mannose-Binding Lectin (MBL) is a member of the collectin family and is an important protein in the immune system. It is a pathogen pattern-recognition molecule that binds to specific carbohydrate motifs on the surface of many pathogens. MBL activates complement via lectin pathway. Single nucleotide polymorphisms in the MBL gene influence serum MBL concentration and function. MBL deficiencies increase the risk of infection and disease-specific complications, especially in those who are already immune compromised with pre-existing conditions. This review discusses the molecular genetics of human MBL and the association of MBL polymorphisms with liver diseases including liver fibrosis, viral hepatitis B, viral hepatitis C, and infection post-liver transplantation.
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