Precursors forms of the isozymes of aspartate aminotransferase from pig heart were synthesized in vitro and purified by binding to specific antibodies. Analysis by sodium dodecylsulfate polyacrylamide gel electrophoresis showed that the precursor of the cytosolic enzyme has similar molecular weight to that of the mature protein whereas the precursor of the mitochondrial isozyme has a molecular weight greater than that of the corresponding mature protein (Delta MW = 2500). Preliminary sequence studies seem to suggest that the precursor of the mitochondrial isozyme has an extra N-terminal peptide sequence while that of the cytosolic protein has only an extra N-terminal Methionine residue.
In vitro synthesis of pig heart aspartate-aminotransferase isoenzymes / Sannia, Giovanni; Abrescia, Paolo; M., Colombo; Giardina, Paola; G. M. A. R. I. N., O.. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 105:(1982), pp. 444-449.
In vitro synthesis of pig heart aspartate-aminotransferase isoenzymes.
SANNIA, GIOVANNI;ABRESCIA, PAOLO;GIARDINA, PAOLA;
1982
Abstract
Precursors forms of the isozymes of aspartate aminotransferase from pig heart were synthesized in vitro and purified by binding to specific antibodies. Analysis by sodium dodecylsulfate polyacrylamide gel electrophoresis showed that the precursor of the cytosolic enzyme has similar molecular weight to that of the mature protein whereas the precursor of the mitochondrial isozyme has a molecular weight greater than that of the corresponding mature protein (Delta MW = 2500). Preliminary sequence studies seem to suggest that the precursor of the mitochondrial isozyme has an extra N-terminal peptide sequence while that of the cytosolic protein has only an extra N-terminal Methionine residue.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
