Identification of G-proteins in rat parotid gland plasma membranes and granule membranes

presence of distinct components in granule membranes

Nawab Ali, Devendra K. Agrawal, Peter Cheung

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

We have identified by immunoblotting and ADP-ribosylation by cholera toxin and pertussis toxin the presence of Mr 43 and 46 KDa G, and 39 and 41 KDa G;.. subunits in rat parotid gland plasma membranes but not in granule membranes. A Mr 28 KDa polypeptide that served as substrate for ADP-ribosylation by both cholera toxin and pertussis toxin was present exclusively in granule membranes. Photoaffinity crosslinking of [α-32P]GTP showed the presence of high molecular weight GTP-binding proteins (Mr 160,100 KDa) in granule membranes. Six low molecular weight GTP-binding proteins (Mr 21-28 KDa) were differentially distributed in both plasma membranes and granule membranes. The present study identifies various GTP-binding proteins in rat parotid gland plasma membranes and granule membranes, and demonstrates the presence of distinct molecular weight GTP-binding proteins in granule membranes. These granule-associated GTP-binding proteins may be involved in secretory processes.

Original languageEnglish
Pages (from-to)155-162
Number of pages8
JournalMolecular and Cellular Biochemistry
Volume115
Issue number2
DOIs
StatePublished - Oct 1992

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Parotid Gland
Cell membranes
GTP-Binding Proteins
Rats
Cell Membrane
Membranes
Molecular Weight
Cholera Toxin
Molecular weight
Pertussis Toxin
Adenosine Diphosphate
Secretory Pathway
Guanosine Triphosphate
Immunoblotting
Crosslinking
Peptides
Substrates

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

Cite this

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title = "Identification of G-proteins in rat parotid gland plasma membranes and granule membranes: presence of distinct components in granule membranes",
abstract = "We have identified by immunoblotting and ADP-ribosylation by cholera toxin and pertussis toxin the presence of Mr 43 and 46 KDa Gsα, and 39 and 41 KDa Giα;.. subunits in rat parotid gland plasma membranes but not in granule membranes. A Mr 28 KDa polypeptide that served as substrate for ADP-ribosylation by both cholera toxin and pertussis toxin was present exclusively in granule membranes. Photoaffinity crosslinking of [α-32P]GTP showed the presence of high molecular weight GTP-binding proteins (Mr 160,100 KDa) in granule membranes. Six low molecular weight GTP-binding proteins (Mr 21-28 KDa) were differentially distributed in both plasma membranes and granule membranes. The present study identifies various GTP-binding proteins in rat parotid gland plasma membranes and granule membranes, and demonstrates the presence of distinct molecular weight GTP-binding proteins in granule membranes. These granule-associated GTP-binding proteins may be involved in secretory processes.",
author = "Nawab Ali and Agrawal, {Devendra K.} and Peter Cheung",
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TY - JOUR

T1 - Identification of G-proteins in rat parotid gland plasma membranes and granule membranes

T2 - presence of distinct components in granule membranes

AU - Ali, Nawab

AU - Agrawal, Devendra K.

AU - Cheung, Peter

PY - 1992/10

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N2 - We have identified by immunoblotting and ADP-ribosylation by cholera toxin and pertussis toxin the presence of Mr 43 and 46 KDa Gsα, and 39 and 41 KDa Giα;.. subunits in rat parotid gland plasma membranes but not in granule membranes. A Mr 28 KDa polypeptide that served as substrate for ADP-ribosylation by both cholera toxin and pertussis toxin was present exclusively in granule membranes. Photoaffinity crosslinking of [α-32P]GTP showed the presence of high molecular weight GTP-binding proteins (Mr 160,100 KDa) in granule membranes. Six low molecular weight GTP-binding proteins (Mr 21-28 KDa) were differentially distributed in both plasma membranes and granule membranes. The present study identifies various GTP-binding proteins in rat parotid gland plasma membranes and granule membranes, and demonstrates the presence of distinct molecular weight GTP-binding proteins in granule membranes. These granule-associated GTP-binding proteins may be involved in secretory processes.

AB - We have identified by immunoblotting and ADP-ribosylation by cholera toxin and pertussis toxin the presence of Mr 43 and 46 KDa Gsα, and 39 and 41 KDa Giα;.. subunits in rat parotid gland plasma membranes but not in granule membranes. A Mr 28 KDa polypeptide that served as substrate for ADP-ribosylation by both cholera toxin and pertussis toxin was present exclusively in granule membranes. Photoaffinity crosslinking of [α-32P]GTP showed the presence of high molecular weight GTP-binding proteins (Mr 160,100 KDa) in granule membranes. Six low molecular weight GTP-binding proteins (Mr 21-28 KDa) were differentially distributed in both plasma membranes and granule membranes. The present study identifies various GTP-binding proteins in rat parotid gland plasma membranes and granule membranes, and demonstrates the presence of distinct molecular weight GTP-binding proteins in granule membranes. These granule-associated GTP-binding proteins may be involved in secretory processes.

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