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http://purl.uniprot.org/citations/2610270http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2610270http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2610270http://www.w3.org/2000/01/rdf-schema#comment"SP-A, a glycoprotein of pulmonary surfactant, consists of an NH2-terminal domain containing a collagen-like sequence and a COOH-terminal domain with sequence homology to several Ca2(+)-dependent lectins. We have compared the size, thermal stability, and secondary structure of recombinant SP-A, the product of a fibroblast line transfected with a single human gene encoding SP-A, with natural SP-A isolated from canine and human lungs. Our results suggest both recombinant and natural SP-A are assembled as large oligomers. More variability in the degree of oligomerization was observed with recombinant human SP-A than with natural canine SP-A. As shown by collagenase digestion, the full assembly of protein subunits was dependent on an intact collagen-like domain. The cysteines in the noncollagen domain of SP-A form intrachain bonds between residues 135-226 and 204-218. The circular dichroism spectra of both recombinant and natural SP-A were consistent with the presence of a collagen-like triple helix. As determined by the change in ellipticity at 205 nm, the thermal transition temperatures of canine, natural human, and recombinant SP-A were 51.5, 52.3, and 42.0 degrees C, respectively. These results suggest differences in the assembly and stability of the natural and recombinant proteins."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.org/dc/terms/identifier"doi:10.1152/ajplung.1989.257.6.l421"xsd:string
http://purl.uniprot.org/citations/2610270http://purl.org/dc/terms/identifier"doi:10.1152/ajplung.1989.257.6.l421"xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Schilling J."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Schilling J."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"White R.T."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"White R.T."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Lau K."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Lau K."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Haagsman H.P."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Haagsman H.P."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Clements J.A."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Clements J.A."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Benson B.J."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Benson B.J."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Hawgood S."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Hawgood S."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Golden J."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/author"Golden J."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/name"Am. J. Physiol."xsd:string
http://purl.uniprot.org/citations/2610270http://purl.uniprot.org/core/name"Am. J. Physiol."xsd:string