Analysis of pulmonary surfactant apoproteins by electrophoresis

Sikandar L. Katyal, Gurmukh Singh

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

Surfactant apoproteins were prepared from detergent-solubilized rat surfactant by immunoaffinity chromatography. SDS-polyacrylamide gel electrophoresis of the apoproteins, without prior chemical reduction, revealed several bands of molecular weights 50 000-78 000, 140 000 and 160 000. Following treatment with dithiothreitol, the apoproteins were resolved into three bands of molecular weights 38 000, 32 000 and 26 000. Further analysis of the apoproteins by two-dimensional polyacrylamide gel electrophoresis showed that each of the proteins of molecular weights 38 000, 32 000 and 26 000 were crosslinked by disulfide bridges and formed homopolymers. Based on periodic acid-Schiff staining, the 38 000 dalton protein appeared to be the richest in carbohydrates, followed by the 32 000 and 26 000 dalton proteins. Partial proteolysis of the 38 000 and 32 000 dalton proteins showed similarity in the sizes of peptides generated. Surfactant-associated proteins from human and monkey lungs were also analyzed by polyacrylamide gel electrophoresis. A non-serum glycoprotein of molecular weight 38 000 was found. In different systems of polyacrylamide gel electrophoresis, this protein showed an electrophoretic mobility similar to that of the 38 000 dalton protein of rat surfactant. However, it formed polymers of molecular weight higher than those of polymers found in rat surfactant.

Original languageEnglish (US)
Pages (from-to)323-331
Number of pages9
JournalBBA - Protein Structure
Volume670
Issue number3
DOIs
StatePublished - Oct 28 1981
Externally publishedYes

Fingerprint

Electrophoresis
Apoproteins
Surface-Active Agents
Molecular Weight
Molecular weight
Proteins
Rats
Polyacrylamide Gel Electrophoresis
Polymers
Proteolysis
Electrophoretic mobility
Periodic Acid
Dithiothreitol
Electrophoresis, Gel, Two-Dimensional
Chromatography
pulmonary surfactant apoprotein
Homopolymerization
Disulfides
Detergents
Haplorhini

Keywords

  • (Human
  • Apoprotein
  • Proteolysis
  • Pulmonary surfactant
  • Rat)

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Analysis of pulmonary surfactant apoproteins by electrophoresis. / Katyal, Sikandar L.; Singh, Gurmukh.

In: BBA - Protein Structure, Vol. 670, No. 3, 28.10.1981, p. 323-331.

Research output: Contribution to journalArticle

@article{39cddf03036a435e8c315e4873e7eab4,
title = "Analysis of pulmonary surfactant apoproteins by electrophoresis",
abstract = "Surfactant apoproteins were prepared from detergent-solubilized rat surfactant by immunoaffinity chromatography. SDS-polyacrylamide gel electrophoresis of the apoproteins, without prior chemical reduction, revealed several bands of molecular weights 50 000-78 000, 140 000 and 160 000. Following treatment with dithiothreitol, the apoproteins were resolved into three bands of molecular weights 38 000, 32 000 and 26 000. Further analysis of the apoproteins by two-dimensional polyacrylamide gel electrophoresis showed that each of the proteins of molecular weights 38 000, 32 000 and 26 000 were crosslinked by disulfide bridges and formed homopolymers. Based on periodic acid-Schiff staining, the 38 000 dalton protein appeared to be the richest in carbohydrates, followed by the 32 000 and 26 000 dalton proteins. Partial proteolysis of the 38 000 and 32 000 dalton proteins showed similarity in the sizes of peptides generated. Surfactant-associated proteins from human and monkey lungs were also analyzed by polyacrylamide gel electrophoresis. A non-serum glycoprotein of molecular weight 38 000 was found. In different systems of polyacrylamide gel electrophoresis, this protein showed an electrophoretic mobility similar to that of the 38 000 dalton protein of rat surfactant. However, it formed polymers of molecular weight higher than those of polymers found in rat surfactant.",
keywords = "(Human, Apoprotein, Proteolysis, Pulmonary surfactant, Rat)",
author = "Katyal, {Sikandar L.} and Gurmukh Singh",
year = "1981",
month = "10",
day = "28",
doi = "10.1016/0005-2795(81)90104-5",
language = "English (US)",
volume = "670",
pages = "323--331",
journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",
issn = "1570-9639",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Analysis of pulmonary surfactant apoproteins by electrophoresis

AU - Katyal, Sikandar L.

AU - Singh, Gurmukh

PY - 1981/10/28

Y1 - 1981/10/28

N2 - Surfactant apoproteins were prepared from detergent-solubilized rat surfactant by immunoaffinity chromatography. SDS-polyacrylamide gel electrophoresis of the apoproteins, without prior chemical reduction, revealed several bands of molecular weights 50 000-78 000, 140 000 and 160 000. Following treatment with dithiothreitol, the apoproteins were resolved into three bands of molecular weights 38 000, 32 000 and 26 000. Further analysis of the apoproteins by two-dimensional polyacrylamide gel electrophoresis showed that each of the proteins of molecular weights 38 000, 32 000 and 26 000 were crosslinked by disulfide bridges and formed homopolymers. Based on periodic acid-Schiff staining, the 38 000 dalton protein appeared to be the richest in carbohydrates, followed by the 32 000 and 26 000 dalton proteins. Partial proteolysis of the 38 000 and 32 000 dalton proteins showed similarity in the sizes of peptides generated. Surfactant-associated proteins from human and monkey lungs were also analyzed by polyacrylamide gel electrophoresis. A non-serum glycoprotein of molecular weight 38 000 was found. In different systems of polyacrylamide gel electrophoresis, this protein showed an electrophoretic mobility similar to that of the 38 000 dalton protein of rat surfactant. However, it formed polymers of molecular weight higher than those of polymers found in rat surfactant.

AB - Surfactant apoproteins were prepared from detergent-solubilized rat surfactant by immunoaffinity chromatography. SDS-polyacrylamide gel electrophoresis of the apoproteins, without prior chemical reduction, revealed several bands of molecular weights 50 000-78 000, 140 000 and 160 000. Following treatment with dithiothreitol, the apoproteins were resolved into three bands of molecular weights 38 000, 32 000 and 26 000. Further analysis of the apoproteins by two-dimensional polyacrylamide gel electrophoresis showed that each of the proteins of molecular weights 38 000, 32 000 and 26 000 were crosslinked by disulfide bridges and formed homopolymers. Based on periodic acid-Schiff staining, the 38 000 dalton protein appeared to be the richest in carbohydrates, followed by the 32 000 and 26 000 dalton proteins. Partial proteolysis of the 38 000 and 32 000 dalton proteins showed similarity in the sizes of peptides generated. Surfactant-associated proteins from human and monkey lungs were also analyzed by polyacrylamide gel electrophoresis. A non-serum glycoprotein of molecular weight 38 000 was found. In different systems of polyacrylamide gel electrophoresis, this protein showed an electrophoretic mobility similar to that of the 38 000 dalton protein of rat surfactant. However, it formed polymers of molecular weight higher than those of polymers found in rat surfactant.

KW - (Human

KW - Apoprotein

KW - Proteolysis

KW - Pulmonary surfactant

KW - Rat)

UR - http://www.scopus.com/inward/record.url?scp=0019802090&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019802090&partnerID=8YFLogxK

U2 - 10.1016/0005-2795(81)90104-5

DO - 10.1016/0005-2795(81)90104-5

M3 - Article

VL - 670

SP - 323

EP - 331

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

SN - 1570-9639

IS - 3

ER -