Structural homologies of cobalamin-binding proteins. Tryptic peptide mapping of intrinsic factor, transcobalamin and haptocorrin from man, hog and rabbit.
We have explored the structural features of cobalamin binding proteins by peptide mapping. The present report is a comparison of the radioiodinated tryptic peptides of intrinsic factor, transcobalamin and haptocorrin from man, hog and rabbit. The results show that the homology between analogous proteins from different species is close for intrinsic factor and transcobalamin and weaker for haptocorrin. The results also suggest the existence of one or more regions which, with minor changes, are conserved among all proteins investigated. This implies a common evolutionary origin for all the cobalamin binding proteins studied.
D000818:Animals; D001798:Blood Proteins / Q000032:analysis*; D006801:Humans; D007437:Intrinsic Factor / Q000032:analysis*; D007457:Iodine Radioisotopes; D010446:Peptide Fragments / Q000302:isolation & purification*; D011489:Protein Denaturation; D011817:Rabbits; D013045:Species Specificity; D013552:Swine; D014155:Transcobalamins / Q000032:analysis*; D014357:Trypsin
D001798:Blood Proteins; D007457:Iodine Radioisotopes; D010446:Peptide Fragments; D014155:Transcobalamins; D007437:Intrinsic Factor; D014357:Trypsin