Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1969 Dec;43(3):480-505.
doi: 10.1083/jcb.43.3.480.

Configuration of a filamentous network in the axoplasm of the squid (Loligo pealii L.) giant nerve fiber

Configuration of a filamentous network in the axoplasm of the squid (Loligo pealii L.) giant nerve fiber

J Metuzals. J Cell Biol. 1969 Dec.

Abstract

High-resolution electron microscopy is integrated with physicochemical methods in order to investigate the following preparations of the giant nerve fibers of the squid (Loligo pealii L.): (1) Thin sections of fibers fixed in four different fixatives; (2) fresh axoplasm stained negatively in solutions of different pH and composition; (3) chemically isolated threadlike elements of the axoplasm. A continuous, three-dimensional network can be identified in all these preparations of the axoplasm. The network is composed of coiled or looped unit-filaments approximately 30 A wide. The unit-filaments are intercoiled in strands approximately 70-250 A wide. The strands are oriented longitudinally in the axoplasm, often having a sinuous course and cross-associations. Microtubules are surrounded by intercoiled unit-filaments and filamentous strands. Calcium ions cause loosening and disintegration of the network configuration. UO(2) (++) ions of a 1% uranyl acetate solution at pH 4.4 display a specific affinity for filamentous protein structures of the squid giant nerve fiber axoplasm, segregating the filamentous elements of the axoplasm in a coiled, threadlike preparation. The uranyl ions combine probably with the carboxyl groups of the main amino acids of the protein-glutamic and aspartic acids. It is proposed that by coiling/decoiling and folding/unfolding of the unit-filaments, shifts in physicochemical properties of the axoplasm are maintained.

PubMed Disclaimer

References

    1. J Gen Physiol. 1957 Mar 20;40(4):635-52 - PubMed
    1. J Physiol. 1957 Sep 30;138(2):253-81 - PubMed
    1. J Cell Biol. 1969 Dec;43(3):456-79 - PubMed
    1. J Gen Physiol. 1960 Mar;43:801-23 - PubMed
    1. J Cell Biol. 1968 Jul;38(1):193-201 - PubMed