Intramembrane particle aggregation in erythrocyte ghosts. I. Effects of protein removal

Journal Article · Tue Jan 01 04:00:00 EST 1974 · J. Cell Biol.; (United States)

DOI:https://doi.org/10.1083/jcb.63.3.1018· OSTI ID:7358694

Elgsaeter, A; Branton, D

We have used freeze-etching and SDS-polyacrylamide gel electrophoresis to study the conditions under which the intramembrane particles of the human erythrocyte ghost may be aggregated. The fibrous membrane protein, spectrin, can be almost entirely removed from erythrocyte ghosts with little or no change in the distribution of the particles. However, after spectrin depletion, particle aggregation in the plane of the membrane may be induced by conditions which cause little aggregation in freshly prepared ghosts. This suggests that the spectrin molecules form a molecular meshwork which limits the translational mobility of the erythrocyte membrane particles.

• Research Organization: Univ. of California, Berkeley
• OSTI ID: 7358694
• Journal Information: J. Cell Biol.; (United States), Journal Name: J. Cell Biol.; (United States) Vol. 63; ISSN JCLBA
• Country of Publication: United States
• Language: English

Related Subjects

550600* -- Medicine
551000 -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
62 RADIOLOGY AND NUCLEAR MEDICINE
ANIMALS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
ELECTRON MICROSCOPY
ELECTROPHORESIS
ERYTHROCYTES
MAMMALS
MAN
MEMBRANES
MICROSCOPY
ORGANIC COMPOUNDS
PARTICLES
PRIMATES
PROTEINS
VERTEBRATES