McIlhinney_1989_Biochem.J_263_387

Reference

Title : A simplified assay for the enzyme responsible for the attachment of myristic acid to the N-terminal glycine residue of proteins, myristoyl-CoA: glycylpeptide N-myristoyltransferase - McIlhinney_1989_Biochem.J_263_387
Author(s) : McIlhinney RA , McGlone K
Ref : Biochemical Journal , 263 :387 , 1989
Abstract :

A greatly simplified assay for myristoyl-CoA:glycylpeptide N-myristoyltransferase (NMT) activity is described. The assay is based on the differential solubility of the acyl-peptides produced as a consequence of the NMT activity and yields results comparable with those obtained with the original assay described by Towler & Glaser [(1986) Proc. Natl. Acad. Sci. U.S.A. 83, 2812-2816], which requires h.p.l.c. to determine the production of the acyl-peptides. The use of the revised assay in the preliminary steps of the purification of rat brain NMT is described, and its use in determining the fatty acid-specificity of the enzyme is illustrated. The results are shown to be comparable with those obtained with the h.p.l.c.-based assay.

PubMedSearch : McIlhinney_1989_Biochem.J_263_387
PubMedID: 2597110

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Citations formats

McIlhinney RA, McGlone K (1989)
A simplified assay for the enzyme responsible for the attachment of myristic acid to the N-terminal glycine residue of proteins, myristoyl-CoA: glycylpeptide N-myristoyltransferase
Biochemical Journal 263 :387

McIlhinney RA, McGlone K (1989)
Biochemical Journal 263 :387