Influence de la méthode de préparation sur les propriétés macromoléculaires de l’actine de carotides de bovidé

Gaspar-Godfroid, A.; Hamoir, G.; Laszt, L.

doi:10.1159/000157716

Cited by 2 publications

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“…The results of this study do not confirm the previous suggestion [1,2,6] that the omission of preextraction of muscle mince with high-ionic-strength solution is essential for the preparation of smooth muscle actin. This is consistent with the fact that both myosin and actin are extractable from smooth muscle with solutions of low as well as high ionic strength [6, [23][24][25][26].…”

Section: Discussioncontrasting

confidence: 99%

“…In a limited number of early studies [1,2,6] on physical and biochemical properties of actins from various smooth muscles their similarity to skeletal muscle actin has been emphasized, although some differences have also been reported. Recently, Suzuki et al [3] described two different forms of chicken gizzard F-actin they obtained depending on whether CaC12 was present or absent during actin purification.…”

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confidence: 99%

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Chicken‐Gizzard Actin: Polymerization and Stability

Strzelecka‐Gołaszewska

Próchniewicz

Nowak

et al. 1980

European Journal of Biochemistry

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Preparations of chicken gizzard actin obtained from acetone-dried muscle powders prepared with various methods developed for skeletal muscle contain variable amounts of a P-actinin-like protein. This contamination is minimized if the procedure of muscle powder preparation includes washing with EDTA solution, and can be completely removed by gel filtration of G-actin on Sephadex G-100. The presence of 8-actinin activity manifests itself in an increased rate of actin polymerization, low filament lengths resulting in low reduced viscosity and enhanced ATP-splitting activity of actin polymer, and instability of the polymer in the absence of free ATP. Gizzard actin purified on a Sephadex G-100 column does not differ from rabbit skeletal muscle actin in its polymerization properties. The distinct property of gizzard actin is the instability of its G form in the absence of added Ca2+, indicating that the affinity of this cation for the single high-affinity site in gizzard actin is lower than in skeletal muscle actin.The procedures generally used to isolate muscle actin involve preparation of acetone-dried muscle powder from which monomeric actin is extracted and purified by reversible polymerization combined with ultracentrifugation. Earlier observations [l -31 indicated that polymerizable actin can be obtained from various vertebrate smooth muscles if the acetone-dried powder is prepared with the method of Carsten and Mommaerts [4]

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Section: Discussioncontrasting

confidence: 99%

mentioning

confidence: 99%

Chicken‐Gizzard Actin: Polymerization and Stability

Strzelecka‐Gołaszewska

Próchniewicz

Nowak

et al. 1980

European Journal of Biochemistry

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“…This low degree of purity is also shown by the tonoactomyosin isolated from cow carotids. It contains 50 % impurities according to Ruegg et al (1965) and some salt-soluble collagen is also extracted at low ionic strength w coprecipitates with this soluble actomyosin (Gaspar-Godfroid, Hamoir & Laszt 1968). These various results make clear that the contractile proteins of smooth muscle are extracted very easily at low ionic strength and that they precipitate at low ionic strength more or less completely according to the pH, together with a large amount of ill-defined globulins typical of the verte brate smooth muscle.…”

Section: T He Extractability Of the Contractile Proteinsmentioning

confidence: 99%

Extractability and properties of the contractile proteins of vertebrate smooth muscle

Hamoir

1973

Phil. Trans. R. Soc. Lond. B

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The vertebrate smooth muscles differ from the striated ones by their larger extracellular space, the smaller size of their cells and their high content in extracellular components. Furthermore, the smooth muscle cell is a bifunctional biological unit able to carry on also an important biosynthetic activity. The contractile proteins of vertebrate smooth muscle are extractable at low ionic strength contrarily to those of striated muscle. The partition of the salt extractable nitrogen between the low and high ionic strength extracts is very different in these two cases. Acidification of low ionic strength extracts of vertebrate smooth muscle at pH 5 allows precipitation of the contractile proteins quantitatively together with a large amount of contaminants typical of the smooth muscles. Comparison of the contractile proteins of vertebrate smooth muscle with their striated counterparts shows that actin is a very constant component of the contractile machinery, that tropomyosin holds an intermediate position, while myosin is the most variable. The smooth muscle myosin differs not only by some general properties as salting-out range and thermostability, but also by the behaviour of various parts of the molecule. The globular head has a different ATPase activity and is responsible for the very peculiar immunological behaviour of this myosin. The point along the myosin rod which is attacked by trypsin is much more resistant to proteolysis. The light meromyosin is more soluble and differs very much in amino acid composition. The comparative study of myosin reveals only minor variations from one species to the other but more or less wide ones within each species according to the type of muscle examined.

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Influence de la méthode de préparation sur les propriétés macromoléculaires de l’actine de carotides de bovidé

Cited by 2 publications

References 0 publications

Chicken‐Gizzard Actin: Polymerization and Stability

Chicken‐Gizzard Actin: Polymerization and Stability

Extractability and properties of the contractile proteins of vertebrate smooth muscle

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