Integrity of the C-terminal part of tyrosine aminotransferase revealed by an anti-peptide serum.
A synthetic peptide corresponding to the seven carboxy-terminal amino acids of tyrosine aminotransferase was coupled to ovalbumin or keyhole limpet haemocyanin, and the resulting conjugates were used to raise anti-peptide antibodies by immunization of rabbits. The crude sera were purified and tested for recognition of the whole enzyme by enzyme-linked immunosorbent assay and immunoprecipitation in extracts from [35S] methionine labeled hepatoma cells. Our results support the existence of an intact C-terminus. If processing takes place, it will rather occur at the N-terminus of this hepatic enzyme.
D000936:Antigen-Antibody Complex; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis; D006433:Hemocyanins; D007106:Immune Sera; D008970:Molecular Weight; D010047:Ovalbumin; D014444:Tyrosine Transaminase / Q000276:immunology / Q000378:metabolism
D000936:Antigen-Antibody Complex; D000939:Epitopes; D007106:Immune Sera; D010047:Ovalbumin; D006433:Hemocyanins; D014444:Tyrosine Transaminase