Analysis of Protein Acylation | Zendy

Jackson Caroline S. | Zendy; Magee Anthony I. | Zendy

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Analysis of Protein Acylation

Author(s) -

Jackson Caroline S.,

Magee Anthony I.

Publication year - 1996

Publication title -

current protocols in protein science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.409

H-Index - 32

eISSN - 1934-3663

pISSN - 1934-3655

DOI - 10.1002/0471140864.ps1402s05

Subject(s) - acylation , biochemistry , chemistry , fatty acid , myristoylation , in vitro , covalent bond , myristic acid , palmitic acid , organic chemistry , phosphorylation , catalysis

Protein acylation is the covalent attachment of fatty acids to a protein; the most commonly added fatty acids are myristate (14:0) and palmitate (16:0). In this unit, protocols describe the use of radiolabeled fatty acids to label eukaryotic cells in vitro. The radiolabeled material produced can then be analyzed by the various methods described here:determination of the type of fatty acid linkage, checking for interconversion by determining the nature of the protein‐bound label, and identification of the protein‐bound fatty acid.

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