Electrospray ionisation studies of the interaction of N,N'-dicyclohexylcarbodiimide with ceroid lipofuscinosis protein (subunit c)
UNSPECIFIED (1997) Electrospray ionisation studies of the interaction of N,N'-dicyclohexylcarbodiimide with ceroid lipofuscinosis protein (subunit c). EUROPEAN MASS SPECTROMETRY, 3 (1). pp. 81-88. ISSN 1356-1049Full text not available from this repository.
N,N'-dicyclohexylcarbodiimide (DCCD) interacts with isolated ceroid lipofuscinosis protein (CLP), a model for subunit c, The products are (a) CLP-DCCD adduct (+206 Dal, presumably by addition at Glu-58; (b) acetyl-CLP-DCCD (+42 Da +206 Dal; (c) acetyl-CLP (+42 Da). Under specific conditions, additional DCCD adducts are formed; CLP-DCCD-DCCD (+206 Da +206 Da) and acetyl-CLP-DCCD-DCCD (+42 Da + 206 Da + 206 Da). Acetylation utilises the acetate present in CLP preparations as a buffer and the site is shown to be located within amino acids 1-9 (probably Lys-7 or N-terminal aspartate), Acetyl-CLP is shown to be the primary product but, in addition, acylation by other fatty acids (myristate, palmitate, oleate and stearate) can be demonstrated in low acetate concentrations, Oligomycin is shown to modify some interactions of CLP with DCCD but venturicidin has little or no effect.
|Item Type:||Journal Article|
|Subjects:||Q Science > QC Physics|
|Journal or Publication Title:||EUROPEAN MASS SPECTROMETRY|
|Number of Pages:||8|
|Page Range:||pp. 81-88|
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