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Chloroform:methanol (2:1) extracts of bovine surfactant were subjected to LH-20 Sephadex chromatography in order to isolate a 6,000-dalton surfactant protein. The 6,000-dalton protein eluted in the void volume and was shown to be homogeneous by protein sequencing, although SDS gel electrophoresis revealed bands of 6, 14, and 18 kDa. The N-terminal sequence obtained was very hydrophobic, as was the amino acid composition of the 6,000-dalton protein. An antiserum raised against the low molecular weight protein fraction from TA surfactant recognized the 6,000-dalton bovine and human proteins in addition to protein bands at 14,000 and 18,000 daltons. These bands appear to be aggregates of the 6,000-dalton protein. No cross-reactivity of the 6,000-dalton protein antiserum could be demonstrated with the 35,000-dalton surfactant-associated protein. These studies strongly suggest that the 35,000- and 6,000-dalton surfactant proteins do not have a precursor-product relationship.
D S Phelps, and
L M Smith, and
H W Taeusch
November 1987,
Proceedings of the National Academy of Sciences of the United States of America,
D S Phelps, and
L M Smith, and
H W Taeusch
June 1988,
The American review of respiratory disease,
D S Phelps, and
L M Smith, and
H W Taeusch
April 1972,
FEBS letters,
D S Phelps, and
L M Smith, and
H W Taeusch
February 1989,
The Journal of biological chemistry,
D S Phelps, and
L M Smith, and
H W Taeusch
October 1983,
International journal of peptide and protein research,
D S Phelps, and
L M Smith, and
H W Taeusch
November 1990,
International journal of peptide and protein research,
D S Phelps, and
L M Smith, and
H W Taeusch
December 1988,
Nucleic acids research,
D S Phelps, and
L M Smith, and
H W Taeusch
July 1988,
Journal of bacteriology,
D S Phelps, and
L M Smith, and
H W Taeusch
January 1985,
The International journal of biochemistry,
D S Phelps, and
L M Smith, and
H W Taeusch
May 1991,
Archives of biochemistry and biophysics,
