Myosin in Polymorphonuclear Leukocytes
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Discussion
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Implication
Laboratory study demonstrates the isolation and characterization of myosin in guinea pig granulocytes, indicating a contractile protein basis for leukocyte motility.
Key Points
- To extract, purify, and biochemically characterize myosin from guinea pig polymorphonuclear leukocytes.
- Homogenized guinea pig granulocytes using either 0.6 M KCl or 0.34 M sucrose solutions.
- Purified protein extracts via low ionic strength precipitation, ammonium sulfate fractionation, and gel filtration chromatography with buffers containing potassium iodide (KI) and ATP.
- Characterized isolated proteins using sodium dodecyl sulfate (SDS) acrylamide gel electrophoresis and rabbit antibody immunodiffusion assays.
- Myosin isolated from sucrose extracts yielded predominantly a single polypeptide chain that co-migrated with skeletal muscle myosin heavy chain on SDS acrylamide gel electrophoresis.
- Rabbit-derived antibodies generated against the purified protein formed a single precipitin line in immunodiffusion tests.
- Preparations derived from 0.6 M KCl cell extracts displayed structural heterogeneity compared to sucrose-extracted isolates.
Cite This Study
Stossel et al. (1973) studied this question.