Structural differences between albumin A and albumin C of the house mouse, Mus musculus.
Two albumins, albumin A from C3H mice and albumin C isolated from descendents of the wild mice in which the variant was first uncovered, were found to differ in their electrophoretic properties. Albumin C was shown to bind two more H+ ions than albumin A at pH 5.4. Peptide mapping after trypsin digestion revealed that albumin C had three peptides (TP-C1, TP-C2, and TP-C3) which were missing in albumin A. The latter likewise had a peptide (TP-A1) which was not found in albumin C. An amino acid analysis of the variant peptides suggests that TP-A1 had been split into TP-C1 and TP-C2 on digestion with trypsin, because a glutamic acid in TP-A1 was replaced by a lysine. This change would also appropriately alter the electrophoretic properties of albumin C. No obvious counterpart was discovered for TP-C3 of albumin C in albumin A.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D014644:Genetic Variation; D005971:Glutamates / Q000032:analysis; D008239:Lysine / Q000032:analysis; D051379:Mice; D008809:Mice, Inbred C3H; D010446:Peptide Fragments / Q000032:analysis; D012709:Serum Albumin; D014357:Trypsin
D000596:Amino Acids; D005971:Glutamates; D010446:Peptide Fragments; D012709:Serum Albumin; D014357:Trypsin; D008239:Lysine