INTERACTION BETWEEN A PROTEIN-BOUND POLYSACCHARIDE (PSK) AND MYOSIN FILAMENTS

We examined the interaction between a protein-bound polysaccharide (PSK) and rabbit skeletal muscle myosin. PSK inhibited the binding of tubulin to myosin in a concentration-dependent manner, whereas it had small effect on actin-myosin interaction as shown by co-sedimentation methods. Native and PSK...

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Bibliographic Details
Published in:Biomedical Research 1987/12/01, Vol.8(6), pp.445-452
Main Authors: FUJII, TOSHIHIRO, SUZUKI, TATSUO, AKASHI, HIROTADA, HOZUMI, TETSU, OGOMA, YOSHIRO, FUJII, MICHIYO, KONDO, YOSHIYUKI
Format: Article
Language:English
Subjects:
Actin
Binding
Chains
Chymotrypsin
Digestion
Filaments
Fragmentation
Fragments
Myosin
Proteolysis
Sedimentation
Skeletal muscle
Trypsin
Tubulin
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Summary:We examined the interaction between a protein-bound polysaccharide (PSK) and rabbit skeletal muscle myosin. PSK inhibited the binding of tubulin to myosin in a concentration-dependent manner, whereas it had small effect on actin-myosin interaction as shown by co-sedimentation methods. Native and PSK-bound myosins were subjected to limited proteolysis with trypsin or chymotrypsin. The digestion patterns were similar between native and PSK-bound myosins. However, PSK binding delayed the digestion of 200 and 130 kDa fragments of heavy chain; also DTNB light chain was not digested by chymotrypsin in the presence of PSK. Electron microscopic observations indicated that myosin filaments in the presence of PSK appeared to be linked to each other and were aligned roughly parallel to the long axis.
ISSN:0388-6107
1880-313X
DOI:10.2220/biomedres.8.445