Polymeric hemoglobins of the house mouse (Mus musculus L.): isolation of cysteinyl peptides.

Abstract

Hemoglobins from wild populations of the house mouse (Mus musculus L.) are polymorphic with respect to the “diffuse” or “single” appearance of their electrophoretic patterns and their ability to form polymers. Polymerization occurs by the formation of intermolecular disulfide bonds. Isolation of all the cysteinyl peptides shows that the reactive cysteinyl residue, β13, is in the same position as that found in BALB/cJ laboratory mice.