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• W1992380230 endingPage "4488" @default.
• W1992380230 startingPage "4484" @default.
• W1992380230 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." @default.
• W1992380230 created "2016-06-24" @default.
• W1992380230 creator A5004905921 @default.
• W1992380230 creator A5062293331 @default.
• W1992380230 date "1979-09-01" @default.
• W1992380230 modified "2023-09-26" @default.
• W1992380230 title "Isolation of a high molecular weight actin-binding protein from baby hamster kidney (BHK-21) cells." @default.
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• W1992380230 doi "https://doi.org/10.1073/pnas.76.9.4484" @default.
• W1992380230 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/411601" @default.
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• W1992380230 hasPublicationYear "1979" @default.
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