Protein sequence analysis studies on the low molecular weight hydrophobic proteins associated with bovine pulmonary surfactant.
Lipid extracts of bovine pulmonary surfactant, which exhibit biophysical and biological activity, contain two hydrophobic proteins which have been designated surfactant protein-B (SP-B) and SP-C. Amino terminal amino acid sequence analysis of whole lipid extracts and partially purified protein fractions gave rise to three sequences, two major and one minor. The first sequence, identified as a member of the SP-B family, extended for 60 amino acids beginning with an amino terminal phe. The second polypeptide, identified as a member of the SP-C family, sequenced for 35 amino acids and had a leu amino terminus. The third minor sequence corresponded to amino acids 2-9 of SP-C (N-leu) and was designated SP-C (N-ile). Sequence analysis of cyanogen bromide peptides derived from methyl isocyanate-blocked lipid extract material produced two peptides which extended the amino acid sequence of SP-B to residue 79, which appears to be a glycine.
Department of Biochemistry and Microbiology, University of Victoria, BC, Canada.
R W
RW
Olafson
U
U
Rink
S
S
Kielland
S H
SH
Yu
J
J
Chung
P G
PG
Harding
F
F
Possmayer
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D008074:Lipoproteins / Q000032:analysis*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D011663:Pulmonary Surfactants / Q000032:analysis*; D012995:Solubility
D008074:Lipoproteins; D010446:Peptide Fragments; D011663:Pulmonary Surfactants