The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual.
The complete amino acid sequence of the single polypeptide chain of human complex-forming glycoprotein heterogeneous in charge (protein HC) isolated from a single individual is reported with the supporting data. The primary structure was determined by automatic degradation of the intact chain and of fragments obtained by chemical and enzymatic degradations of the native or reduced and S-carboxymethylated protein. The polypeptide chain of protein HC contained 182 amino acid residues with a calculated molecular weight of 20,621. No amino acid sequence variability was found and such variability can therefore not explain the great charge heterogeneity of protein HC in a single individual. The amino acid sequence of protein HC was nearly identical to the one reported for human alpha 1-microglobulin in a research communication but contained 15 additional residues.
D000510:Alpha-Globulins / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D006801:Humans; D010446:Peptide Fragments
D000510:Alpha-Globulins; D010446:Peptide Fragments; C016001:alpha-1-microglobulin