Literature DB >> 2934003

Purification of synexin by pH step elution from chromatofocusing media in the absence of ampholytes.

J H Scott, K L Kelner, H B Pollard.   

Abstract

Synexin can be purified to virtual homogeneity by a modification of the conventional chromatofocusing technique. Ampholytes are omitted from the procedure altogether and the protein is eluted by a specific pH step chosen on the basis of the pI of the protein. This modification of the conventional method eliminates the separation of ampholytes from the purified protein, an insurmountable problem in our case, and reduces the cost of purification profoundly.

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Year:  1985        PMID: 2934003     DOI: 10.1016/0003-2697(85)90489-0

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  2 in total

1.  Calcium channel activity of purified human synexin and structure of the human synexin gene.

Authors:  A L Burns; K Magendzo; A Shirvan; M Srivastava; E Rojas; M R Alijani; H B Pollard
Journal:  Proc Natl Acad Sci U S A       Date:  1989-05       Impact factor: 11.205

2.  Ca2+-activated synexin forms highly selective, voltage-gated Ca2+ channels in phosphatidylserine bilayer membranes.

Authors:  H B Pollard; E Rojas
Journal:  Proc Natl Acad Sci U S A       Date:  1988-05       Impact factor: 11.205

  2 in total

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