Electron microscope study of native and crosslinked rabbit muscle phosphofructokinase.

Published

Journal Article

Electron microscopy of native and dimethyl-suberimidate crosslinked rabbit muscle phosphofructokinase (EC 2.7.1.11; 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.

Full Text

Duke Authors

Cited Authors

  • Telford, JN; Lad, PM; Hammes, GG

Published Date

  • August 1, 1975

Published In

Volume / Issue

  • 72 / 8

Start / End Page

  • 3054 - 3056

PubMed ID

  • 127174

Pubmed Central ID

  • 127174

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.72.8.3054

Language

  • eng

Conference Location

  • United States