Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein

Joanna Floros, R. Steinbrink, K. Jacobs, David Phelps, R. Kriz, M. Recny, L. Sultzman, S. Jones, H. W. Taeusch, H. A. Frank

Research output: Contribution to journalArticle

133 Citations (Scopus)

Abstract

A group of 35,000-dalton sialoglycoproteins is the major non-serum protein component of pulmonary surfactant. Tryptic fragments of these proteins were sequenced, and oligonucleotide probes were synthesized based on the amino acid sequences. A human lung cDNA library was then screened using the oligonucleotide probes, and clones coding for these proteins were identified and characterized. By in vitro transcription-translation experiments we have associated individual clones with particular proteins. The data suggest that co-translational modifications of two primary translation products account for many of the isoforms observed by two-dimensional gel electrophoresis in the precursors of 35,000-dalton sialoglycoproteins.

Original languageEnglish (US)
Pages (from-to)9029-9033
Number of pages5
JournalJournal of Biological Chemistry
Volume261
Issue number19
StatePublished - Dec 1 1986

Fingerprint

Pulmonary Surfactant-Associated Proteins
Complementary DNA
Clone Cells
Sialoglycoproteins
Oligonucleotide Probes
Proteins
Pulmonary Surfactants
Electrophoresis, Gel, Two-Dimensional
Transcription
Electrophoresis
Gene Library
Amino Acid Sequence
Protein Isoforms
Gels
Amino Acids
Lung
Experiments

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Floros, Joanna ; Steinbrink, R. ; Jacobs, K. ; Phelps, David ; Kriz, R. ; Recny, M. ; Sultzman, L. ; Jones, S. ; Taeusch, H. W. ; Frank, H. A. / Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein. In: Journal of Biological Chemistry. 1986 ; Vol. 261, No. 19. pp. 9029-9033.
@article{97529d938f4347e4bac559707335f2bd,
title = "Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein",
abstract = "A group of 35,000-dalton sialoglycoproteins is the major non-serum protein component of pulmonary surfactant. Tryptic fragments of these proteins were sequenced, and oligonucleotide probes were synthesized based on the amino acid sequences. A human lung cDNA library was then screened using the oligonucleotide probes, and clones coding for these proteins were identified and characterized. By in vitro transcription-translation experiments we have associated individual clones with particular proteins. The data suggest that co-translational modifications of two primary translation products account for many of the isoforms observed by two-dimensional gel electrophoresis in the precursors of 35,000-dalton sialoglycoproteins.",
author = "Joanna Floros and R. Steinbrink and K. Jacobs and David Phelps and R. Kriz and M. Recny and L. Sultzman and S. Jones and Taeusch, {H. W.} and Frank, {H. A.}",
year = "1986",
month = "12",
day = "1",
language = "English (US)",
volume = "261",
pages = "9029--9033",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "19",

}

Floros, J, Steinbrink, R, Jacobs, K, Phelps, D, Kriz, R, Recny, M, Sultzman, L, Jones, S, Taeusch, HW & Frank, HA 1986, 'Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein', Journal of Biological Chemistry, vol. 261, no. 19, pp. 9029-9033.

Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein. / Floros, Joanna; Steinbrink, R.; Jacobs, K.; Phelps, David; Kriz, R.; Recny, M.; Sultzman, L.; Jones, S.; Taeusch, H. W.; Frank, H. A.

In: Journal of Biological Chemistry, Vol. 261, No. 19, 01.12.1986, p. 9029-9033.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein

AU - Floros, Joanna

AU - Steinbrink, R.

AU - Jacobs, K.

AU - Phelps, David

AU - Kriz, R.

AU - Recny, M.

AU - Sultzman, L.

AU - Jones, S.

AU - Taeusch, H. W.

AU - Frank, H. A.

PY - 1986/12/1

Y1 - 1986/12/1

N2 - A group of 35,000-dalton sialoglycoproteins is the major non-serum protein component of pulmonary surfactant. Tryptic fragments of these proteins were sequenced, and oligonucleotide probes were synthesized based on the amino acid sequences. A human lung cDNA library was then screened using the oligonucleotide probes, and clones coding for these proteins were identified and characterized. By in vitro transcription-translation experiments we have associated individual clones with particular proteins. The data suggest that co-translational modifications of two primary translation products account for many of the isoforms observed by two-dimensional gel electrophoresis in the precursors of 35,000-dalton sialoglycoproteins.

AB - A group of 35,000-dalton sialoglycoproteins is the major non-serum protein component of pulmonary surfactant. Tryptic fragments of these proteins were sequenced, and oligonucleotide probes were synthesized based on the amino acid sequences. A human lung cDNA library was then screened using the oligonucleotide probes, and clones coding for these proteins were identified and characterized. By in vitro transcription-translation experiments we have associated individual clones with particular proteins. The data suggest that co-translational modifications of two primary translation products account for many of the isoforms observed by two-dimensional gel electrophoresis in the precursors of 35,000-dalton sialoglycoproteins.

UR - http://www.scopus.com/inward/record.url?scp=0023000540&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023000540&partnerID=8YFLogxK

M3 - Article

C2 - 3755136

AN - SCOPUS:0023000540

VL - 261

SP - 9029

EP - 9033

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 19

ER -