The animal and human plasma membrane (Ca(2+)+Mg2+)-ATPases--approaches to molecular arrangements of functional parts and oxidative changes.
The molecular structures of animal and human plasma membrane (Ca(2+)+Mg2+)-ATPases are not completely understood in part due to the fact that no suitable single crystal is available. The elucidation of the two-dimensional structure is in progress. The amino acid sequences of human erythrocyte and rat plasma membrane Ca2+ pump isoforms as well as of the pig smooth muscle plasma membrane Ca2+ pump are already known. This article reviews the present state of the knowledge in (Ca(2+)+Mg2+)-ATPase research of animal and human plasma membranes performed in the past few years, concerning in particular arrangements of proteolytically cleaved fragments, and relations between the erythrocyte (Ca(2+)+Mg2+)-ATPase in situ and the purified red cell enzyme, oxidative changes. Results of different experimental approaches concerning the structure of (Ca(2+)+Mg2+)-ATPases rather than the applications of the methods used are emphasized.
Földes-Papp
Z
Z
University of Ulm, Section for Polymers, Ulm (Donau), West Germany.
D000818:Animals; D001665:Binding Sites; D055592:Biophysical Phenomena; D001703:Biophysics; D017301:Ca(2+) Mg(2+)-ATPase / Q000737:chemistry / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000737:chemistry / Q000378:metabolism* / Q000502:physiology; D002462:Cell Membrane / Q000201:enzymology*; D004910:Erythrocyte Membrane / Q000201:enzymology; D006801:Humans; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010766:Phosphorylation
D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases