[Characterization of liver tyrosine aminotransferase in rats using an immunoaffinity technic].
Antisera directed against synthetic peptides with sequences that correspond to selected regions of tyrosine aminotransferase may react with the protein without affecting its biological activity. The antiserum against the theoretical N-terminal dodecapeptide recognizes the enzyme and makes it possible to detect a blocked form of the enzyme. Another form shortened by seven aminoacids and starting with Thr 8 has been found. The isolation of tyrosine aminotransferase by one step affinity chromatography is now made possible; nevertheless the elution procedure remains a critical point. The strategy described should have further applications and allow the detailed exploration of the essential domains of aminotransferases, especially those involved in the function and the degradation of pyridoxal phosphate requiring enzymes.
Dietrich
J B
JB
Laboratoire de Biochemie, Institut de Biologie moléculaire et cellulaire, C.N.R.S., Strasbourg.
Beck
G
G
D000818:Animals; D002846:Chromatography, Affinity / Q000379:methods; D008099:Liver / Q000201:enzymology*; D010443:Peptide Chain Termination, Translational; D051381:Rats; D014444:Tyrosine Transaminase / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism
D014444:Tyrosine Transaminase
Caractérisation de la tyrosine aminotransférase de foie de rat par une technique d'immunoaffinité.