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Determination of N-myristoyl Peptide Sequence Both by MALDI TOF MASS and With an N-myristoyl Cleaving Enzyme (Polymyxin Acylase)

Determination of N-myristoyl Peptide Sequence Both by MALDI TOF MASS and With an N-myristoyl Cleaving Enzyme (Polymyxin Acylase)

S Misumi, M Tsuruta, K Furuishi, S Shoji

Biochem Biophys Res Commun. 1995 Dec 14;217(2):632-9.

PMID: 7503745

Abstract:

Polymyxin acylase isolated from Pseudomonas sp. M-6-3 was used as an N-myristoyl cleaving enzyme in order to determine a part of the N-terminal amino acid sequence of N-myristoyl proteins. The enzyme hydrolyzed a number of N-myristoyl oligopeptides at various hydrolysis rates but not N-myristoyl proteins. The oncogenic protein (N-myristoyl-pp60c-src) was isolated from human colon adenocarcinoma cell line COLO 320DM by two-dimensional polyacrylamide gel electrophoresis. The protein was digested with trypsin and the resultant tryptic N-myristoyl tetrapeptide (N-myristoyl-Gly-Ser-Asn-Lys) was purified by HPLC and the structure was determined both by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI TOF MASS) and by a gas-phase protein sequencer before or after treatment with the polymyxin acylase. The results suggest that the N-myristoyl peptide sequence derived from N-myristoyl proteins was clearly determined by the combined use of MALDI TOF MASS and the N-myristoyl cleaving enzyme.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP111174437	Polymyxin Acylase from Pseudomonas sp.		111174-43-7	Price

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