Nature of the multiple forms of alanine aminopeptidase.
Alanine aminopeptidase (particle-bound aminopeptidase, EC 3.4.11.2) isolated in a highly purified state from human liver, kidney, and pancreas were investigated with regard to their different electrophoretic mobilities. While the molecular weights are identical, different isoelectric points were found. The results of carbohydrate analysis point to N-acetylneuraminic acid as the main factor that causes the differences in electrophoretic behaviour of the alanine aminopeptidases investigated.
D000606:Amino Sugars / Q000032:analysis; D000626:Aminopeptidases; D002241:Carbohydrates / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D005643:Fucose / Q000032:analysis; D005690:Galactose / Q000032:analysis; D005947:Glucose / Q000032:analysis; D006801:Humans; D007526:Isoelectric Point; D007668:Kidney / Q000201:enzymology*; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D009928:Organ Specificity; D010179:Pancreas / Q000201:enzymology*; D012794:Sialic Acids / Q000032:analysis
D000606:Amino Sugars; D002241:Carbohydrates; D012794:Sialic Acids; D005643:Fucose; D000626:Aminopeptidases; D005947:Glucose; D005690:Galactose