Electron microscope study of native and crosslinked rabbit muscle phosphofructokinase.
Journal Article (Journal Article)
Electron microscopy of native and dimethyl-suberimidate crosslinked rabbit muscle phosphofructokinase (EC 184.108.40.206; ATP:D-fructose-6-phosphate 1-phosphotransferase) has been carried out using negative staining with sodium phosphotungstate. The results obtained suggest the protomer of molecular weight 80,000 can be approximated as a prolate ellipsoid with axes of 67 A and 25 A. The dimer, which is the fundamental unit for polymerization, is formed by association along the 25 A axis and has approximately dimensions of 67 A X 55 A X 25 A. The tetramer appears to be formed by an end-to-end aggregation of dimers, and the octamer is a sheet-like structure made up of a side-to-side aggregation of tetramers. Higher crosslinked aggregates and long crosslinked filaments also are seen. The filaments have a constant width of about 250 A, are about 0.5 mum in length, and appear to involve tetramers as a fundamental structural unit. The functional significance of the filament structure is not known.
- Telford, JN; Lad, PM; Hammes, GG
- August 1, 1975
Volume / Issue
- 72 / 8
Start / End Page
- 3054 - 3056
Pubmed Central ID
International Standard Serial Number (ISSN)
Digital Object Identifier (DOI)
- United States