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Coexpression of proteins with methionine aminopeptidase and/or N-myristoyltransferase inEscherichia colito Increase acylation and homogeneity of protein preparations

Authors
Publisher
Elsevier Science & Technology
Identifiers
DOI: 10.1016/s0076-6879(02)44715-5
Keywords
  • Section Ii. Isolation Or Production Of Native Or Modified G Protein Subunits
Disciplines
  • Biology

Abstract

Abstract New plasmid constructs described in this article allow the coexpression in bacteria of any protein with several different NMT proteins, including the recently cloned full-length human NMT 1 and 2, I s and with increased expression of bacterial Met-AP Through the use of these plasmids in different combinations it should be possible to improve the homogeneity of a large number of recombinant protein preparations by the complete removal of the initiating methionine and increased extent of N-myristoylation. The new reagents described in this article are available upon request.

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