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Proceedings Paper

Studies of the interactions between calcium-binding proteins and phosphofructokinase using fluorescent probes
Author(s): Jianqing Lan; Robert F. Steiner
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Paper Abstract

Phosphofructokinase (PFK) is a calmodulin (CaM) binding protein (Mayr, G.W. and Heilmeyer , L.M.G., Jr (1983) FEBS Lett. 195, 51)..We found that troponin C (TnC), which is homologous to CaM, also binds PFK. PFK titration of AEDANS-TnC showed that their apparent dissociation constant is comparable to that of PFK-CaM. Fluorescent labels were used to probe contact regions on TnC and CaM. It is likely that the C-terminal end of the connecting strand of the TnC molecule is close to PFK in the binary complex. Hydrophobic regions of TnC and CaM also possibly play roles in the binding and in the polymerization of PFK.

Paper Details

Date Published: 1 May 1990
PDF: 11 pages
Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); doi: 10.1117/12.17749
Show Author Affiliations
Jianqing Lan, Univ. of Maryland/Baltimore County (United States)
Robert F. Steiner, Univ. of Maryland/Baltimore County (United States)

Published in SPIE Proceedings Vol. 1204:
Time-Resolved Laser Spectroscopy in Biochemistry II
Joseph R. Lakowicz, Editor(s)

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