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Journal of the Korean Society of Neonatology 1999;6(1):1-7.
Published online January 1, 2001.
Purification and Analysis of Amino Acid Sequences of Pulmonary Surfactant Proteins.
Chong Woo Bae, Yong Mook Choi
Abstract
PURPOSE
For the synthesis of surfactant protein(SP) peptides and production of next generation artificial pulmonary surfactant(PS), we have isolated SP-B, C from bovine PS, and studied the biochemical properties and amino acid sequences of these protein-peptides.
METHODS
Crude surfactant and purified surfactant were isolated from materials extracted from the bovine lung lavage. The hydrophobic SP-B, C were purified by Sephadex LH 60 column chromatography from PS. The purities of SP-B, C were assessed by tricine buffer SDS-polyacrylamide gel electrophoresis and the amino acid sequences of these proteins were determined using Beckman PI-2090.
RESULTS
The molecular weights of SP-B, C shown in SDS-polyacrylamide gel electrophoresis were as follows; 15,000-18,000(oligomer) Da for SP-B, 3,500-5,000 Da for SP-C. The amino acid sequences were; FPIPLPYCWL LRTLIKKIQA VIPKGVLAMT VAQCHVVPL LVGGIQQLV IEYSVILLTD TLLGRLPNLV CGLRLRCSG in SP-B, LIPCCPVNIK RLLIVVVVVV LLVVVIVGAL LMGL in SP-C, respectively. These results indicated that the amino acid sequences of bovine SPs were different.
CONCLUSION
The SP-B, C were purified from bovine PS, and amino acid sequences of SP-B, C were determined. Further studies are needed for the development and use of next generations of exogenous PS preparation based on synthetic SP-peptides for the treatment of neonatal RDS in the future.
Key Words: Pulmonary surfactant, Surfactant protein(SP), SP-B, C, Peptides, Respiratory distress syndrome(RDS), Newborn infants
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