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Human uridine monophosphate synthase: baculovirus expression, immunoaffinity column purification and characterization of the acetylated amino terminus

Authors :
Han, Byoung-Don
Livingstone, Laura R.
Pasek, Daniel A.
Yablonski, Michael J.
Jones, Mary Ellen
Source :
Biochemistry. August 29, 1995, Vol. 34 Issue 34, p10835, 9 p.
Publication Year :
1995

Abstract

The N-terminal sequence of pure human uridine monophosphate synthase is modified in vitro and that changes involve removal of N-terminal methionine residue from the gene-coded sequence and subsequent acetylation of the formerly penultimate alanine residue to yield acetyl-AVAR as the acetylated N-terminal tetrapeptide. Purified protein expressed in cabbage looper (Tricoplusiani) larvae expressing human cDNA also begins with the N-terminal acetyl-AVAR.

Details

ISSN :
00062960
Volume :
34
Issue :
34
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.17962615