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- W2394304895 abstract "To analyze the primary structure of a slow electrophoretic hemoglobin at Zhaoyuan city,Shandong,the purified abnormal chain was hydrolyzed by TPCK Trypsin,the abnormal peptide was separated by HPLC,and its amino acids composition and sequence were analyzed.Data showed the abnormal peptide was the same as normal β 41→59 peptide.No reaction took place between the abnormal peptide and CNBr.With the mass spectrophy analysis,the abnormal peptide showed a peak of mass charge ratio of 1 038 and the normal only a peak of mass charge ratio of 1 030.It appeard that the β 55 Met of the abnormal peptide was converted to the sulfoxide form β 55 Met·O.The change of primary structure was the structural basis of the slow electrophoretic Hb.It might be called Hb Zhaoyuan." @default.
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- W2394304895 date "1999-01-01" @default.
- W2394304895 modified "2023-09-27" @default.
- W2394304895 title "Structural analysis of a hemoglobin with beta 55 Met sulfoxide" @default.
- W2394304895 hasPublicationYear "1999" @default.
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