Literature DB >> 2775255

Prenylated proteins: demonstration of a thioether linkage to cysteine of proteins.

H C Rilling1, E Bruenger, W W Epstein, A A Kandutsch.   

Abstract

Prenylated amino acid fragments have been isolated from prenylated proteins of Chinese hamster ovary cells. Gel-exclusion chromatography indicates that these proteins are modified by two different prenyl groups. The prenyl-amino acid fragments are labeled by 35S from cysteine, and this bond is cleaved by Raney-Ni, proving that the prenyl residue is linked to protein via a thioether to cysteine. Hydrazinolysis has been used to demonstrate that the cysteine is carboxy terminal.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2775255     DOI: 10.1016/0006-291x(89)92111-6

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  Quantitation of prenylcysteines by a selective cleavage reaction.

Authors:  W W Epstein; D Lever; L M Leining; E Bruenger; H C Rilling
Journal:  Proc Natl Acad Sci U S A       Date:  1991-11-01       Impact factor: 11.205

2.  Prenylated proteins: synthesis of geranylgeranylcysteine and identification of this thioether amino acid as a component of proteins in CHO cells.

Authors:  W W Epstein; D C Lever; H C Rilling
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

3.  Purification and characterization of recombinant human farnesyl diphosphate synthase expressed in Escherichia coli.

Authors:  V D Ding; B T Sheares; J D Bergstrom; M M Ponpipom; L B Perez; C D Poulter
Journal:  Biochem J       Date:  1991-04-01       Impact factor: 3.857

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.