Over many years, the protein components of pulmonary surfactant have been the subject of a large number of analyses using high resolution methods for protein analysis. In fact, identification of protein biomarkers for lung disorder is extremely important in order to gain insight into the mechanisms underlying lung diseases. For separation of protein components of pulmonary surfactant proteins, two-dimensional gel electrophoresis (2-DE) coupled with Western blot analysis involving electrophoretic transfer of the separated proteins onto a membrane followed by immunodetection of proteins by enhanced chemiluminescence has been used. This method allows very high resolution, sensitivity and specificity for proteomic study of pulmonary surfactant-associated proteins, particularly for water-soluble surfactant-associated protein-A (SP-A). Analysis of SP-A has also been carried out with 2-DE followed by either amino acid sequence analysis using Edman degradation or mass spectrometry. Other pulmonary surfactant-associated proteins, SP-B, SP-C and SP-D were identified using either gel electrophoresis based or non-gel-electrophoresis based methods, such as high performance liquid chromatography. This review summarizes the major achievements in proteomic studies of pulmonary surfactantassociated proteins.
Keywords: Human pulmonary surfactant proteins, bronchoalveolar lavage fluid proteins, two-dimensional gel electrophoresis, polymorphism
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