Comparative studies of two types of bovine immunoglobulin G heavy chains.
;Fingerprints' of bovine colostrum and serum immunoglobulin G1 heavy chains were extremely similar, but different from serum immunoglobin G2 heavy chains. Serum immunoglobulin G1 and immunoglobulin G2 heavy chains were treated with cyanogen bromide. The fractions from the C-terminal end of the heavy chains were isolated and the amino acid sequence of this fraction from immunoglobulin G2 was:His-Glx-Ala-Leu-His-Asx-His-Tyr-Met-Gln-Lys-Ser-Thr-Ser-Lys-Ser-Ala-GlyThe amino acid composition of this fraction from immunoglobulin G1 was the same except for the methionine, which in immunoglobulin G1 was replaced by threonine.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D003126:Colostrum / Q000032:analysis; D003486:Cyanides; D004586:Electrophoresis; D010084:Oxidation-Reduction; D010455:Peptides / Q000032:analysis; D014357:Trypsin; D005719:gamma-Globulins / Q000032:analysis*
D000596:Amino Acids; D003486:Cyanides; D010455:Peptides; D005719:gamma-Globulins; D014357:Trypsin