Sandor Papp
University of Pennsylvania
13 Papers
163 Citations
Sandor Papp is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Quenching (fluorescence) & Phosphorescence. The author has an hindex of 8, co-authored 13 publications. Previous affiliations of Sandor Papp include State University of New York System.
Chat about Author
Papers
Fluorescence energy transfer as an indicator of Ca2+-ATPase interactions in sarcoplasmic reticulum.
TL;DR: The technique is suitable for kinetic analysis of the effect of various treatments on the monomer-oligomer equilibrium of Ca2+-ATPase, and a drawback is that the labeled ATPase, although it retains conformational responses, is enzymatically inactive.
45
Reactions of excited triplet states of metal substituted myoglobin with dioxygen and quinone.
TL;DR: No difference was seen in triplet quenching by oxygen for either derivative, indicating that differences in the polypeptide chain between the two derivatives are not large enough to affect oxygen penetrability.
45
•Journal Article
Structure of Ca2+-ATPase in sarcoplasmic reticulum.
Anthony Martonosi,László Dux,Kenneth A. Taylor,H.P. Ting-Beall,S Varga,P. Csermely,N Mullner,Sandor Papp,Istvan Jona +8 more
TL;DR: In this paper, the morphology of sarcoplasmic reticulum, classification of Ca(2+)-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology is reviewed.
33
The effect of chelating agents on the elemental composition of sarcoplasmic reticulum: the reactivity of SH groups with N-(1-pyrene)maleimide.
TL;DR: Observations suggest that Zn2+ may play a role in the regulation of the reactivity of SH groups in sarcoplasmic reticulum either by direct interaction with cysteinyl residues or by an effect upon the conformation of a subpopulation of ATPase molecules.
12
Tryptophan phosphorescence of the Ca2+-ATPase of sarcoplasmic reticulum.
TL;DR: Phosphorescence of protein tryptophan was analyzed in sarcoplasmic reticulum vesicles, and in the purified Ca2+ transport ATPase in deoxygenated aqueous solutions at room temperature; the quenching by ATP showed saturation consistent with the idea that the ATP-enzyme complex had a lower phosphorescence yield.
11