ArticleProceedings of the National Academy of Sciences of the United States of America1979
Isolation of a high molecular weight actin-binding protein from baby hamster kidney (BHK-21) cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1979. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 37 citations in OpenAlex.
- A novel protein accumulated during maturation of the pods of the plant Impatiens balsamina.Molecular and cellular biochemistry · 1994Article
- Probing the mechanism of incorporation of fluorescently labeled actin into stress fibers.The Journal of cell biology · 1986Article
- Suppression of tropomyosin synthesis, a common biochemical feature of oncogenesis by structurally diverse retroviral oncogenes.Molecular and cellular biology · 1985Article
- Dual effect of filamin on actomyosin ATPase activity.Journal of muscle research and cell motility · 1985Article
- Purification of a high molecular weight actin filament gelation protein from Acanthamoeba that shares antigenic determinants with vertebrate spectrins.The Journal of cell biology · 1984Article
- Contribution of actin to the structure of the cytoplasmic matrix.The Journal of cell biology · 1984Review
- Isolation and characterization of a high molecular weight actin-binding protein from Physarum polycephalum plasmodia.The Journal of cell biology · 1984Article
- An immunocytochemical study of intraneuronal inclusions of the caudate and substantia nigra. Reaction with an anti-actin antiserum.Acta neuropathologica · 1982Article
- Isolation and characterization of actin and actin-binding protein from human platelets.The Journal of cell biology · 1981Article
- Fluorescence photobleaching recovery in solutions of labeled actin.Biophysical journal · 1981Article
- Microfilaments and tropomyosin of cultured mammalian cells: isolation and characterization.The Journal of cell biology · 1980Article
- Subplasmalemmal linear densities in cells of the mononuclear phagocyte system in lung.The American journal of pathology · 1980Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A high molecular weight protein (HMWP) with properties similar to those of both actin-binding protein (ABP) and filamin has been isolated from cultured baby hamster kidney (BHK-21) cells. The protein was present in an actomyosin-depleted sucrose extract of the cells and was eluted, upon gel chromatography on Sepharose 4B, near the void volume. The subunit migration on sodium dodecyl sulfate/polyacrylamide gels and the amino acid composition of HMWP were similar to those of ABP and filamin. HMWP bound to and crosslinked F-actin from rabbit muscle, as shown by the formation of a gel that was sedimented with low-speed centrifugation. This interaction was insensitive to temperature and low concentrations of calcium ions, although it may depend on the presence of myosin. Observation of thin sections of the actin-HMWP gel revealed crosslinked complexes of laterally aggregated actin filaments. The axial period of the dense crosslinks was 34 nm. The HMWP may be involved in regulation of microfilament organization.
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