Literature DB >> 1120160

Demonstration of a class of proteins loosely associated with secretory granule membranes.

M R Robinovitch, P J Keller, J Iversen, D L Kauffman.   

Abstract

It is shown, in this study, that rat secretory granule membrane preparations, as prepared by the method of Amsterdam et al. [(1971) J. Cell Biol. 50, 187-200], contain a protein fraction which is removed by washing in isotonic medium. This fraction contains unusually high levels of Pro, Gly and Glx, and appears to label rapidly if the rats are pulsed with [14-c] amino acids prior to removal of the glands. The fraction, which may represent specifically adsorbed secretory protein(s) or peripheral membrane protein, is significant to investigators using this model system to study secretory phenomena.

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Year:  1975        PMID: 1120160     DOI: 10.1016/0005-2736(75)90184-4

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  5 in total

1.  Isolation and compositional analysis of secretion granules and their membrane subfraction from the rat parotid gland.

Authors:  R S Cameron; J D Castle
Journal:  J Membr Biol       Date:  1984       Impact factor: 1.843

2.  Isolation and partial characterization of two populations of secretory granules from rat parotid glands.

Authors:  J M Iversen; D L Kauffman; P J Keller; M Robinovitch
Journal:  Cell Tissue Res       Date:  1985       Impact factor: 5.249

3.  Chemical and physical characterization of a phosphoprotein, Protein C, from human saliva and comparison with a related protein A.

Authors:  A Bennick
Journal:  Biochem J       Date:  1977-05-01       Impact factor: 3.857

Review 4.  Salivary proline-rich proteins.

Authors:  A Bennick
Journal:  Mol Cell Biochem       Date:  1982-06-11       Impact factor: 3.396

5.  The binding of calcium to a salivary phosphoprotein, protein A, common to human parotid and submandibular secretions.

Authors:  A Bennick
Journal:  Biochem J       Date:  1976-04-01       Impact factor: 3.857

  5 in total

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