Title of article
Purification and characterization of cytoplasmic dynein of rabbit liver
Author/Authors
Ko Nakajima، نويسنده , , Masafumi Komatsu، نويسنده , , Itaru Toyoshima، نويسنده , , Tomoyuki Kuramitsu، نويسنده , , Tsuyoshi Ono، نويسنده , , Masato Funaoka، نويسنده , , Junji Kato، نويسنده , , Osamu Masamune، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1995
Pages
5
From page
66
To page
70
Abstract
Cutplasmic dynein is a microtubule-dependent motor protein, which plays a role in intracellular transport. However, there have been a few studies regarding the role of cytoplasmic dynein in the liver. Purification of cytoplasmic dynein from rabbit liver took advantage of the affinity of microtubule-dependent motor proteins for microtubules. Purified dynein contained heavy chain (450 kDa), intermediate chain (75 kDa), light chains (45–58 kDa) and dynactin (150 kDa). The subunit composition was consistent with previously reported data on brain cytolplasmic dynein. Microtubules prepared from bovine brain were driven by purified cytoplasmic dynein from rabbit liver, and movements of microtubules were visualized by video-enhanced differential interference contrast microscopy. The mean velocity of the motile microtubules was 1.09±0.13 μm/s. Our study provides evidence of rapid intracellular transport in hepatocytes controlled by cytoplasmic dynein.
Keywords
Intracellulartransport , Microtubules. , Cytoplasmic dynein , Hepatocyte
Journal title
Journal of Hepatology
Serial Year
1995
Journal title
Journal of Hepatology
Record number
580886
Link To Document