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J. Biol. Chem., Vol. 266, Issue 16, 10099-10103, Jun, 1991
Y Minami, H Kawasaki, Y Miyata, K Suzuki and I Yahara
The 90-kDa heat shock protein, HSP90, of the mouse has two isoforms, alpha
and beta, which are electrophoretically separable. We have investigated the
native forms of HSP90 molecules under physiological conditions and
determined their isoform compositions. Analysis by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis showed that HSP90 purified from
mouse lymphoma L5178Y cells consists of approximately 40% alpha and 60%
beta isoforms. Analysis by nondenaturing polyacrylamide gel electrophoresis
showed that the purified HSP90 exists predominantly as a dimer, but a
considerable amount of monomer was also detected. Western blotting using
polyclonal anti-mouse HSP90 antibodies revealed that the native forms of
HSP90 in the crude L5178Y cell lysates are also dimer and monomer. The
nondenaturing polyacrylamide gel electrophoresis resolved the dimeric forms
into two separate bands that were identified as alpha/alpha and beta/beta
homodimers by two methods: sodium dodecyl sulfate- polyacrylamide gel
electrophoresis and peptide mapping. In addition, the results showed that
the monomeric form consists mainly of the beta isoform. Both the alpha and
beta isoforms were shown to bind equally to actin filaments.
Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90
Department of Cell Biology, Tokyo Metropolitan Institute of Medical Science, Japan.
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