Structural determination of a new electrophoreticaly silent variant: hemoglobin Alzette, beta 104(G6)Arg --> Lys.
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.
Promé
D
D
Laboratoire de Pharmacologie et Toxicologie Fondamentales du CNRS, Toulouse, France.
Promé
J C
JC
Déon
C
C
Groff
P
P
Kalmes
G
G
Galacteros
F
F
Wajcman
H
H
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D005914:Globins / Q000737:chemistry / Q000302:isolation & purification; D006455:Hemoglobins, Abnormal / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification; D014357:Trypsin
C101182:Hemoglobin Alzette; D006455:Hemoglobins, Abnormal; D010455:Peptides; D005914:Globins; D014357:Trypsin