Integrity of the C-terminal part of tyrosine aminotransferase revealed by an anti-peptide serum.

Abstract:

: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.

authors

Dietrich JB,Genot G,Beck G

doi

10.1016/s0006-291x(87)80035-9

subject

Has Abstract

pub_date

1987-04-29 00:00:00

pages

801-6

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(87)80035-9

journal_volume

144

pub_type

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