| Autor: |
Shelley, S., Balis, J., Paciga, J., Espinoza, C., Richman, A. |
| Zdroj: |
Lung; 1982, Vol. 160 Issue 1, p195-206, 12p |
| Abstrakt: |
Surfactant was isolated from minced adult human lung tissues by repetitive centrifugation on NaBr density gradients. The surface active fraction contained 12 mg phospholipid per mg of protein. Eighty percent of the phospholipid was phosphatidylcholine and 9% was phosphatidylglycerol. The phosphatidylcholines, 55% of which were disaturated, contained more than 70% palmitic acid. In contrast, phosphatidylglycerol contained 22% palmitic acid and 52% oleic acid, suggesting that the importance of phosphatidylglycerol in surfactant function relates to its acidic head group. The most abundant proteins in human surfactant were high molecular weight (>400,000) glycoproteins which on reduction with dithiothreitol yielded peptides of 34,000 daltons. Antibodies to the high molecular weight proteins were prepared in rabbits and using immunoperoxidase methods were shown to stain alveolar type II cells and the alveolar and bronchial surfaces, but no other human tissues. A low molecular weight protein was also present in lung surfactant and was most apparent in surfactant subfractions which had higher phospholipid to protein ratios. The results of this study provide a basis to further investigate the role of normal and altered surfactant constituents in disease states of the human lung. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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