The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues

Author:

Doonan S1,Doonan H J1,Hanford R1,Vernon C A1,Walker J M1,Airold L P da S.1,Bossa F2,Barra D2,Carloni M2,Fasella P2,Riva F2

Affiliation:

1. The Christopher Ingold Laboratories, Department of Chemistry, University College London, 20 Gordon Street, London WC1HOAJ, U.K.

2. Istituto di Chimica Biologica e Centro de Biologia Molecolare del Consiglio Nazionale delle Ricerche, Università di Roma, Città Universitaria, 00185 Roma, Italy

Abstract

Carboxymethylated aspartate aminotransferase was digested with a proteinase claimed to be specific for lysine residues. Complete cleavage occurred at 12 of the 19 lysine residues in the protein, but at the remaining seven residues cleavage was either restricted or absent. In addition, cleavage was observed at three of the 26 arginine residues. These results are discussed with reference to the amino acid residues adjacent to points of complete or restricted cleavage. The complete primary structure of aspartate aminotransferase, based on these and other studies, is given. Evidence for the assignment of some acid and amide side chains has been deposited as Supplementary Publication SUP 50050 (11 pp.) at the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975) 145, 5. The evidence for the assignment of residue 366 was less conclusive than for the other acid and amide side chains and is, therefore, given in the main paper.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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