Drosophilia spectrin. I. Characterization of the purified protein.

Journal Article

We purified a protein from Drosophila S3 tissue culture cells that has many of the diagnostic features of spectrin from vertebrate organisms: (a) The protein consists of two equimolar subunits (Mr = 234 and 226 kD) that can be reversibly cross-linked into a complex composed of equal amounts of the two subunits. (b) Electron microscopy of the native molecule reveals two intertwined, elongated strands with a contour length of 180 nm. (c) Antibodies directed against vertebrate spectrin react with the Drosophila protein and, similarly, antibodies to the Drosophila protein react with vertebrate spectrins. One monoclonal antibody has been found to react with both of the Drosophila subunits and with both subunits of vertebrate brain spectrin. (d) The Drosophila protein exhibits both actin-binding and calcium-dependent calmodulin-binding activities. Based on the above criteria, this protein appears to be a bona fide member of the spectrin family of proteins.

Full Text

Duke Authors

Cited Authors

  • Dubreuil, R; Byers, TJ; Branton, D; Goldstein, LS; Kiehart, DP

Published Date

  • November 1987

Published In

Volume / Issue

  • 105 / 5

Start / End Page

  • 2095 - 2102

PubMed ID

  • 3680372

International Standard Serial Number (ISSN)

  • 0021-9525

Language

  • eng

Conference Location

  • United States