ISSN:
1573-4927
Keywords:
mouse hemoglobin
;
neutral amino acid substitution
;
isoelectric focusing
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The primary structures of the α globins from CE/J, DBA/2J, and a stock of Potter's mice were determined to identify the amino acid substitutions associated with the unique isoelectric focusing patterns of these hemoglobins. In addition, the primary structures of the α globins from MOL III and PERU mice were studied in search of amino acid substitutions that may not be detected by isoelectric focusing. CE/J hemoglobin contains a unique kind of α globin called chain 5. It differs from the single kind of α globin (chain 1) in C57BL/6 by having alanine rather than glycine at position 78. DAB/2J hemoglobin has two kinds of α globins: one half is like chain 5 and the other half is like chain 1. The hemoglobin from Potter's stock of Mus musculus molossinus also contains chains 1 and 5, but they are expressed at different levels, i.e., 80% chain 1 and 20% chain 5. MOL III hemoglobin has a single kind of α globin identical to that in C57BL/6, and PERU hemoglobin contains approximately 40% chain 1 and 60% chain 4. Chains 1 and 4 have different amino acids at positions 25, 62, and 68. These studies confirm that mouse hemoglobins separable by isoelectric focusing, but not by other means of electrophoresis, have substitutions of neutrally charged amino acids in their α chains.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00484946
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