Purification and partial characterization of analogous 26-kDa rat submandibular and parotid gland integral membrane phosphoproteins that may have a role in exocytosis

Rat submandibular and parotid gland exocytosis is primarily controlled by β-adrenergic receptor stimulation. Although its precise role in the regulation of salivary gland exocytosis is not fully understood, protein phosphorylation, mediated by the activation of cAMP-dependent protein kinase, may be...

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Veröffentlicht in:Archives of oral biology 1992-04, Vol.37 (4), p.289-295
Hauptverfasser: Quissell, D.O., Deisher, L.M.
Format: Artikel
Sprache:eng
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Zusammenfassung:Rat submandibular and parotid gland exocytosis is primarily controlled by β-adrenergic receptor stimulation. Although its precise role in the regulation of salivary gland exocytosis is not fully understood, protein phosphorylation, mediated by the activation of cAMP-dependent protein kinase, may be directly involved. Previous studies suggest that analogous 26-kDa integral membrane phosphoproteins may play a direct role in regulating exocytosis. Studies were here undertaken to purify and partially characterize both phosphoproteins. After endogeneous phosphorylation with 32P, subcellular fraction and solubilization of the microsomal fraction in n-octyl β-glucopyranoside, the 26-kDa integral membrane phosphoproteins were purified by high performance liquid chromatography (HPLC), followed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and electroelution of the proteins. Amino acid analysis indicated a significant number of serine amino acids: N-terminal sequence data demonstrated a high level of homology; and trypsin digestion followed by reversed-phase HPLC indicated the possibility of multiple phosphorylation sites.
ISSN:0003-9969
1879-1506
DOI:10.1016/0003-9969(92)90051-9