Studies of the interactions between calcium-binding proteins and phosphofructokinase using fluorescent probes

Jianqing Lan; Robert F. Steiner

doi:10.1117/12.17749

1 May 1990 Studies of the interactions between calcium-binding proteins and phosphofructokinase using fluorescent probes

Jianqing Lan, Robert F. Steiner

Author Affiliations +

Proceedings Volume 1204, Time-Resolved Laser Spectroscopy in Biochemistry II; (1990) https://doi.org/10.1117/12.17749
Event: OE/LASE '90, 1990, Los Angeles, CA, United States

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.

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Jianqing Lan and Robert F. Steiner "Studies of the interactions between calcium-binding proteins and phosphofructokinase using fluorescent probes", Proc. SPIE 1204, Time-Resolved Laser Spectroscopy in Biochemistry II, (1 May 1990); https://doi.org/10.1117/12.17749

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