Search PubMed⌕ Search

Biomedical subjects

G Metz

Publications and source records attributed to G Metz.

92 records · Page 6Linked to original sources
PubMedDate not supplied

The quaternary structure of yeast aminopeptidase I. 1. Molecular forms and subunit size.

The smallest active form of aminopeptidase I (EC 3.4.11.1) from yeast has a molecular weight of 6.4 X 10(5). At neutral pH the active enzyme is in equilibrium with two inactive subfragments (Mr = 3.2 X 10(5) and 1.1 X 10(5)) as well as with higher aggregates (Mr greater than or equal 1.2 X 10(6)). All of these species may be dissociated to give a single type of subunits with a molecular weight of 5.3 X 10(4). It is concluded that the active enzyme is a dodecamer whereas the subfragments correspond to dimeric and hexameric forms.

Aminopeptidases↗
PubMedDate not supplied

The quaternary structure of yeast aminopeptidase I. 2. Geometric arrangement of subunits.

Electron micrographs of native aminopeptidase I and of isolated subfragments were taken after negative staining with uranyl formate. From these studies and from the chemical evidence summarized in the preceding paper it is concluded that the active enzyme is a dodecamer possessing pseudo-D3 symmetry with the dimer as the smallest symmetric unit.

Aminopeptidases↗