Stiffness of carbodiimide-crosslinked glycerinated muscle fibres in rigor and relaxing solutions at high salt concentrations

1986 ◽  
Vol 7 (4) ◽  
pp. 339-350 ◽  
Author(s):  
Katsuhisa Tawada ◽  
Michio Kimura
Keyword(s):  
High Salt ◽  
Muscle Fibres ◽  
Glycerinated Muscle

scholarly journals In situ reconstitution of myosin filaments within the myosin-extracted myofibril in cultured skeletal muscle cells.

1982 ◽  
Vol 92 (2) ◽  
pp. 324-332 ◽  
Author(s):  
M Taniguchi ◽  
H Ishikawa
Keyword(s):  
Skeletal Muscle ◽  
Salt Solution ◽  
Muscle Cells ◽  
High Salt ◽  
Skeletal Muscle Cells ◽  
Thin Filaments ◽  
Skeletal Muscle Myosin ◽  
Myosin Filaments ◽  
Glycerinated Muscle

We studied the in situ reconstitution of myosin filaments within the myosin-extracted myofibrils in cultured chick embryo skeletal muscle cells using the electron microscope and polarization microscope. Myosin was first extracted from the myofibrils in glycerinated muscle cells with a high-salt solution containing 0.6 M KCl. When rabbit skeletal muscle myosin was added to the myosin-extracted cells in the high-salt solution, thin filaments in the ghost myofibrils were bound with myosin to form arrowhead complexes. Subsequent dilution of KCl in the myosin solution to 0.1 M resulted in the formation of thick myosin filaments within the myofibrils, increasing the birefringence of the myofibrils. When Mg-ATP was added such myosin-reassembled myofibrils were induced either to form supercontraction bands or to restore the sarcomeric arrangement of thick and thin filaments. Under the polarization microscope, vibrational movement of the myofibrils was seen transiently upon addition of Mg-ATP, often resulting in a regular arrangement of myofibrils in register. These myofibrils, with reconstituted myosin filaments, structurally and functionally resembled the native myofibrils. The findings are discussed with special reference to the myofibril formation in developing muscle cells.

scholarly journals Modification of the interactions of myosin with actin and 5′-adenylyl imidodiphosphate by substitution of ethylene glycol for water

1984 ◽  
Vol 217 (1) ◽  
pp. 169-177 ◽  
Author(s):  
S B Marston ◽  
R T Tregear
Keyword(s):  
Ethylene Glycol ◽  
Dissociation Rate ◽  
Detectable Effect ◽  
Muscle Fibres ◽  
Skeletal Muscle Myosin ◽  
Specific Effects ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Glycerinated Muscle ◽  
Myosin X

We studied the effect of replacing water by ethylene glycol as solvent on the properties of skeletal muscle myosin, myosin subfragment-1 (S1) and heavy meromyosin. Ethylene glycol (50%, v/v) had no detectable effect on the affinity of myosin or actomyosin for the substrate analogue 5′-adenylyl imidodiphosphate (AMPPNP). However, the rate constants for formation and dissociation of the myosin X MgAMPPNP complex were reduced 200-fold; the logarithm of the dissociation rate was roughly proportional to the fractional concentration of ethylene glycol. Nucleotide dissociation was accelerated at least 300-fold by pure actin but remained slow with regulated actin in the absence of Ca2+. Ethylene glycol substitution reduced the affinity of S1 and the S1 X MgAMPPNP complex for actin equally (100-fold at 50% ethylene glycol). These results show that ethylene glycol has specific effects on myosin's enzymic mechanism, which can account for its effect on the tension and stiffness of glycerinated muscle fibres.

The Relation Between VIIIR:AG and VIII:C Studied with Two Antisera

1979 ◽  
Author(s):  
H. P. Muller ◽  
N. H. van Tilburg ◽  
R. M. Bertina ◽  
J. J. Veltkamp
Keyword(s):  
Molecular Weight ◽  
High Salt ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Specific Antibodies ◽  
Specific Effects ◽  
Normal Plasma ◽  
Coagulant Activity ◽  
Sterical Hindrance ◽  
Inhibitory Antibodies

FVIII was separated into low molecular weight FVIII (LMW FVIII) and high molecular weight FVIII (HMW FVIII) by gel chromatography in the presence of high salt concentration or by high salt elution of LMW FVIII from FVIII bound to anti HMW FVII-Sepharose. Specific antibodies were raised in rabbits against HMW FVIII and LMW FVIII. After removal of the contaminating anti HMW activities the rabbit anti LMW FVIII was still able to neutralize the FVIII coagulant activity of normal plasma and of IMW FVIII with canparable efficiency and it had no effect on the VIIIR:WF of FVIII in normal plasma or in HMW FVIII. Anti LMW FVIII does not bind to HMW FVIII and does not precipitate FVIII as tested by counter immunoelectrophoresis. Rabbit anti HMW FVIII precipitates FVIII in normal plasma, inhibits VIIIR:WF activity, while it has no effect on the FVIII coagulant activity of LMW FVIII. The coagulant activity of FVIII in normal plasma is slightly inhibited by anti HMW FVIII presumably by non-specific effects (sterical hindrance). It is concluded that inhibitory antibodies against VIII:C raised in rabbits recognize antigenic structures only present on LMW FVIII. Antibodies against HMW FVIII raised in rabbits appears to recognize structures only present on HMW FVIII.

463-P: Deterioration of Atherosclerosis via Dysbiosis in ApoE Null Mice Fed with High-Salt Diet

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 463-P
Author(s):  
TOMONORI KIMURA ◽  
YOSHITAKA HASHIMOTO ◽  
TAKAFUMI SENMARU ◽  
EMI USHIGOME ◽  
MASAHIDE HAMAGUCHI ◽  
...  
Keyword(s):  
High Salt ◽  
High Salt Diet ◽  
Salt Diet
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