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Hemoglobin southampton (Casper): Characterization of the base mutation
Author(s) -
Heintz Nicholas H.,
Howard Phillip L.
Publication year - 1989
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830300102
Subject(s) - cytidine , restriction enzyme , mutation , restriction site , cpg site , hemoglobin , dna , microbiology and biotechnology , genetics , globin , biology , mutation testing , chemistry , gene , biochemistry , enzyme , dna methylation , gene expression
Hemoglobin Casper is characterized by the substitution of cytidine for thymidine in condon 106 of the beta globin gene. This substitution results in the creation of a new restriction site for Msp I but not for the isoschizimer Hpa II. The restriction pattern following digestion with Msp I reveals a 9.9‐kb fragment not seen in normal individuals or following digestion of Casper DNA with Hpa II. This finding confirms the predicted base mutation and indicates that the cytidine in the newly acquired CpG site is methylated.