Erythrocyte actin and spectrin. Interactions with muscle contractile and regulatory proteins
| Autor: | Jonathan Maimon, Saul Puszkin, Elena Puszkin |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Erythrocytes
Biophysics Arp2/3 complex Tropomyosin macromolecular substances Myosins Binding Competitive Biochemistry Contractile Proteins Myosin Humans Actinin Spectrin Actin-binding protein Adenosine Triphosphatases biology Chemistry Erythrocyte Membrane Temperature Membrane Proteins EPB41 Actin remodeling Cell Biology Actins Troponin biology.protein MDia1 Protein Binding |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 513:205-220 |
| ISSN: | 0005-2736 |
| Popis: | Actin and spectrin were isolated from washed red blood cell membranes. Spectrin bound and polymerized erythrocyte actin in the absence of potassium. Spectrin coated onto polystyrene latex particles bound 8–9 mol of erythrocyte actin per mol of spectrin when actin was in its depolymerized state. Spectrin enhanced the interaction of erythrocyte actin with muscle myosin as manifested by changes in Mg2+-ATPase activity. A similar enhancement also was observed with muscle α-actinin while muscle tropomyosin abolished these effects. The data suggest that spectrin may play the role of polymerizing factor as well as the anchoring site for erythrocyte actin just as α-actinin is the anchoring site for actin filaments in muscle and other non-muscle cells. |
| Databáze: | OpenAIRE |
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