Structural comparison of several actin-binding macromolecules
Journal Article
·
· J. Cell Biol.; (United States)
The cytoskeletal components, macrophage actin-binding protein and filamin were dried from glycerol and examined by low-angle rotary shadowing electron microscopy. Both are elongate, flexible molecules whose general morphology is similar to that of erythrocyte spectrin. Neither actin-binding protein nor filamin binds to spectrin-depleted erythrocyte membranes.
- Research Organization:
- Harvard Univ., Cambridge, MA
- OSTI ID:
- 5375229
- Journal Information:
- J. Cell Biol.; (United States), Journal Name: J. Cell Biol.; (United States) Vol. 85:2; ISSN JCLBA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550200* -- Biochemistry
551000 -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
ACTIN
ANIMAL CELLS
BIOCHEMISTRY
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CELL CONSTITUENTS
CELL MEMBRANES
CHEMISTRY
COMPARATIVE EVALUATIONS
CONNECTIVE TISSUE CELLS
ELECTRON MICROSCOPY
ERYTHROCYTES
MACROPHAGES
MATERIALS
MEMBRANES
MICROSCOPY
MOLECULAR STRUCTURE
MORPHOLOGY
ORGANIC COMPOUNDS
PHAGOCYTES
PROTEINS
SOMATIC CELLS
551000 -- Physiological Systems
59 BASIC BIOLOGICAL SCIENCES
ACTIN
ANIMAL CELLS
BIOCHEMISTRY
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CELL CONSTITUENTS
CELL MEMBRANES
CHEMISTRY
COMPARATIVE EVALUATIONS
CONNECTIVE TISSUE CELLS
ELECTRON MICROSCOPY
ERYTHROCYTES
MACROPHAGES
MATERIALS
MEMBRANES
MICROSCOPY
MOLECULAR STRUCTURE
MORPHOLOGY
ORGANIC COMPOUNDS
PHAGOCYTES
PROTEINS
SOMATIC CELLS