Structural determination of a new electrophoreticaly silent variant: hemoglobin Alzette, beta 104(G6)Arg --Lys

Autor:	D, Promé, J C, Promé, C, Déon, P, Groff, G, Kalmes, F, Galacteros, H, Wajcman
Rok vydání:	1995
Předmět:	Molecular Weight Hemoglobins Abnormal Molecular Sequence Data Humans Trypsin Amino Acid Sequence Peptides Chromatography High Pressure Liquid Globins
Zdroj:	Rapid communications in mass spectrometry : RCM.
ISSN:	0951-4198
Popis:	A new electrophoreticaly neutral hemoglobin variant was found by ion-exchange high-performance liquid chromatography (HPLC). The molecular mass of the beta-chain was shifted down 28 mass units. The modification was found in the beta T-11 peptide that co-elutes with beta T-14 in the tryptic HPLC profile. Collision-induced decomposition of the protonated modified peptide indicated the Arg --Lys exchange at the C-terminus. This modifies the fragmentation pattern as charge-remote processes induced by the strong basicity of arginine were replaced by charge-induced mechanisms. The exchanged 104Arg is one of the chloride binding sites in the central cavity of Hb.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::4908496dd02fbe2607b228baf8485e6a https://pubmed.ncbi.nlm.nih.gov/8829478 Zobrazit plný text záznamu Plný text