TY - JOUR
T1 - Purification and properties of Mg2+ Ca2+ adenosinetriphosphatase from Escherichia coli
AU - Nelson, N.
AU - Kanner, B. I.
AU - Gutnick, D. L.
PY - 1974
Y1 - 1974
N2 - A procedure for the purification of Mg2 Ca2 adenosinetriphosphatase (EC 3.6.1.3) from E. coli, yielding relatively large amounts of highly active enzyme, is described. The enzyme consists of 4 non identical subunits. Trypsin treatment of purified enzyme yields a preparation consisting exclusively of the 2 larger subunits, which are sufficient for ATPase activity. Purified enzyme is inhibited by 7 chloro 4 nitrobenzo 2 oxa 1,3 diazole; this inhibition is reversed by dithiothreitol, and the diazole is found preferentially associated with the β subunit of the enzyme. Antibody prepared against the trypsin treated enzyme inhibited various ATP dependent reactions as well as membrane bound ATPase itself.
AB - A procedure for the purification of Mg2 Ca2 adenosinetriphosphatase (EC 3.6.1.3) from E. coli, yielding relatively large amounts of highly active enzyme, is described. The enzyme consists of 4 non identical subunits. Trypsin treatment of purified enzyme yields a preparation consisting exclusively of the 2 larger subunits, which are sufficient for ATPase activity. Purified enzyme is inhibited by 7 chloro 4 nitrobenzo 2 oxa 1,3 diazole; this inhibition is reversed by dithiothreitol, and the diazole is found preferentially associated with the β subunit of the enzyme. Antibody prepared against the trypsin treated enzyme inhibited various ATP dependent reactions as well as membrane bound ATPase itself.
UR - http://www.scopus.com/inward/record.url?scp=0016085918&partnerID=8YFLogxK
U2 - 10.1073/pnas.71.7.2720
DO - 10.1073/pnas.71.7.2720
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AN - SCOPUS:0016085918
SN - 0027-8424
VL - 71
SP - 2720
EP - 2724
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 7
ER -