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Purification, characterization and partial amino acid sequences of carnitine palmitoyl‐transferase from human liver
Author(s) -
Gaetano Finocchiaro,
Irma Colombo,
Stefano DiDonato
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81354-q
Subject(s) - carnitine , biochemistry , transferase , enzyme , human liver , peptide sequence , pig liver , microbiology and biotechnology , amino acid , antibody , biology , protein subunit , peptide , affinity chromatography , chemistry , gene , genetics
Carnitine palmitoyl‐transferase has been extracted with 0.5% Tween‐20 from human liver homogenatc and purified to homogeneity. The purified enzyme has a native M r of 274 kDa. The subunit M r is of 66 kDa, as shown by SDS‐PAGE and immunoblots obtained with antibodies raised against human CPT. Purified CPT shows high affinity for palmitoyl‐CoA and palmitoyl‐carnitine and is not inhibited by malonyl‐CoA, Seven tryptic peptides and the N‐terminal of purified human CPT have been sequenced, and found homologous to rat CPT sequence. Both antibodies and peptide sequences are important tools for the investigation of the molecular basis of CPT deficiency in man.