Literature DB >> 7864829

Sheep pancreatic microsomes as an alternative to the dog source for studying protein translocation.

M A Kaderbhai1, V J Harding, A Karim, B M Austen, N N Kaderbhai.   

Abstract

A procedure is described for the preparation of rough membrane vesicles of endoplasmic-reticular origin from the pancreas of sheep. These isolated membranes translocate, process and glycosylate in vitro-translated heterologous proteins in a manner comparable with that exhibited by dog pancreatic microsomes.

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Year:  1995        PMID： 7864829      PMCID： PMC1136481          DOI： 10.1042/bj3060057

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  25 in total

Review 1.  The role of organelles in the chemical modification of the primary translation products of secretory proteins.

Authors:  P N Campbell; G Blobel
Journal:  FEBS Lett       Date:  1976-12-31       Impact factor: 4.124

2.  Hen oviduct signal peptidase is an integral membrane protein.

Authors:  M O Lively; K A Walsh
Journal:  J Biol Chem       Date:  1983-08-10       Impact factor: 5.157

3.  Design and synthesis of a consensus signal sequence that inhibits protein translocation into rough microsomal vesicles.

Authors:  B M Austen; J Hermon-Taylor; M A Kaderbhai; D H Ridd
Journal:  Biochem J       Date:  1984-11-15       Impact factor: 3.857

4.  A method for rapid isolation of rough and smooth microsomes and Golgi apparatus from rat liver in the same sucrose gradient.

Authors:  P O Sandberg; L Marzella; H Glaumann
Journal:  Exp Cell Res       Date:  1980-12       Impact factor: 3.905

5.  Dog pancreatic microsomal-membrane polypeptides analysed by two-dimensional gel electrophoresis.

Authors:  M A Kaderbhai; B M Austen
Journal:  Biochem J       Date:  1984-01-01       Impact factor: 3.857

6.  Processing of chimeric mammalian cytochrome b5 precursors in Escherichia coli: reaction specificity of signal peptidase and identification of an aminopeptidase in post-translocational processing.

Authors:  V Harding; A Karim; N Kaderbhai; A Jones; A Evans; M A Kaderbhai
Journal:  Biochem J       Date:  1993-08-01       Impact factor: 3.857

7.  Yeast pheromone alpha-factor is synthesized as a high molecular weight precursor.

Authors:  O Emter; B Mechler; T Achstetter; H Müller; D H Wolf
Journal:  Biochem Biophys Res Commun       Date:  1983-11-15       Impact factor: 3.575

8.  Prepro-alpha-factor has a cleavable signal sequence.

Authors:  M G Waters; E A Evans; G Blobel
Journal:  J Biol Chem       Date:  1988-05-05       Impact factor: 5.157

9.  Secretion in yeast: translocation and glycosylation of prepro-alpha-factor in vitro can occur via an ATP-dependent post-translational mechanism.

Authors:  J A Rothblatt; D I Meyer
Journal:  EMBO J       Date:  1986-05       Impact factor: 11.598

10.  Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.

Authors:  P Walter; I Ibrahimi; G Blobel
Journal:  J Cell Biol       Date:  1981-11       Impact factor: 10.539
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  3 in total

1.  A mammalian cytochrome fused to a chloroplast transit peptide is a functional haemoprotein and is imported into isolated chloroplasts.

Authors:  Y Y Liu; N Kaderbhai; M A Kaderbhai
Journal:  Biochem J       Date:  2000-10-15       Impact factor: 3.857

2.  Membrane integration of Sec61alpha: a core component of the endoplasmic reticulum translocation complex.

Authors:  B C Knight; S High
Journal:  Biochem J       Date:  1998-04-01       Impact factor: 3.857

3.  Bat3 promotes the membrane integration of tail-anchored proteins.

Authors:  Pawel Leznicki; Anne Clancy; Blanche Schwappach; Stephen High
Journal:  J Cell Sci       Date:  2010-06-01       Impact factor: 5.285
  3 in total

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