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Immunocytochemical localization of myosin in rabbit liver cell.
Author(s) -
T Ueno,
Shinichi Yasuura,
Satoru Watanabe,
Miyoko Hirose,
T Sekine,
T Namihisa
Publication year - 1988
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/36.7.3290335
Subject(s) - myosin , actin , myosin light chain kinase , immunofluorescence , immunocytochemistry , skeletal muscle , biology , antibody , microbiology and biotechnology , immunoglobulin light chain , staining , chemistry , biochemistry , anatomy , endocrinology , immunology , genetics
It has been established that the liver cell possesses its own myosin which resembles other non-muscle myosins in subunit composition and in its dependence of actin-activated Mg2+-ATPase activity on light chain phosphorylation (Ueno T, Sekine T: Biochem Int, 1987;15:1205). We have raised a specific antibody against rabbit liver cell myosin. Immunoblot analysis has shown that the purified antibody reacts only with the heavy chain of liver cell myosin. The antibody did not react with rabbit skeletal muscle myosin or with smooth muscle myosin extracted from rabbit intestinal wall. Cryostat liver sections analyzed by indirect immunofluorescence microscopy showed a characteristic polygonal staining pattern, indicating that myosin is concentrated close to the plasma membrane, particularly in the region of bile canaliculi. Myosin therefore appears to be localized in the area where actin filaments are also abundant.

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