Characterization of the murine corticosteroid binding globulin: variations between mammalian forms.
Corticosteroid binding globulin (CGB) from term-pregnant mouse serum was isolated and characterized by peptide analysis after treatment with CNBr and Lys-specific protease, respectively. Amino acid sequence analysis of six segments, covering 189 of 383 positions in different regions of the protein, showed unexpectedly low overall homology (60%) to the indirectly deduced human amino acid sequence previously reported. However, some segments displayed a greater resemblance to their human counterparts. Differences were observed in at least two of six potential glycosylation sites. The nature of electrophoretic CBG variants and their immunological properties are described.
Nyberg
L
L
Department of Chemistry I, Karolinska Institute, Stockholm, Sweden.
Marekov
L N
LN
Jones
I
I
Lundquist
G
G
Jörnvall
H
H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003488:Cyanogen Bromide; D010450:Endopeptidases; D005260:Female; D014644:Genetic Variation; D006031:Glycosylation; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D011247:Pregnancy; D012689:Sequence Homology, Nucleic Acid; D014156:Transcortin / Q000235:genetics
D000596:Amino Acids; D014156:Transcortin; D010450:Endopeptidases; C044574:lysine-C peptidase; D003488:Cyanogen Bromide