Ward E. Harris

TL;DR: The labelled (Na+ +K+)-ATPase (ATP phosphohydrolase, EC 3.6.1.3), although reversibly inhibited, was capable of undergoing conformational changes associated with the active enzyme that could be monitored fluorometrically and suggest that the enzyme can change conformational states in the presence of appropriate ligands.

TL;DR: The ouabain-binding capacity and the ouABain-membrane complex were more stable than the (Na + ,K + )-ATPase activity to treatment with agents known to affect the membrane integrity, such as, NaClO 4, sodium dodecyl sulfate, p- chloromercuribenzoate, urea.

TL;DR: A procedure using the two SH reagents sequentially seems to permit a more selective labelling of the SH groups involved in the (Na+ + K+)-ATPase than is possible by using MalNEt alone.

TL;DR: Observations indicate how the conformation of a biological membrane might be altered by the interaction between acidic phospholipids and calcium.

TL;DR: It is proposed that cis-parinaric acid, like fatty acids normally found in brain, is incorporated into membrane phospholipids by an acyl-CoA acyltransferase, and the presence of this enzyme in nervous tissue may make it possible to easily introduce fluorescent fatty acid probes into membrane phosphate membranes and to thereby facilitate study of membrane-mediated processes.