Superprecipitation induced by soluble myosin fragments

Avraham Oplatka, Julian Borejdo, Hanna Gadasi

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Superprecipitation (s.p.) took place when both an active myosin fragment [heavy meromyosin (HMM) or HMM subfragment-1 (S-1)] and an inactivated myosin were added to actin. The duration of the "clearing phase" decreased, while the rate and extent of s.p. increased up to a constant value when the myosin fragment concentration was raised. The extent and rate were higher while the delay time shorter for HMM, as compared to S-1 at the same concentration, No s.p. could be detected when: a) an inactivated myosin fragment or the ATPase apyrase was used; b) MgATP was replaced by Mg-pyrophosphate; c) the ability of myosin to form "rigor" complex with actin has been abolished. It is concluded that the soluble myosin fragment is probably involved in the mechanochemical process associated with s.p..

Original languageEnglish
Pages (from-to)1323-1328
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume66
Issue number4
DOIs
StatePublished - 27 Oct 1975

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Myosin Subfragments
Myosins
Actins
Apyrase
Adenosine Triphosphatases
Adenosine Triphosphate
Time delay

Cite this

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title = "Superprecipitation induced by soluble myosin fragments",
abstract = "Superprecipitation (s.p.) took place when both an active myosin fragment [heavy meromyosin (HMM) or HMM subfragment-1 (S-1)] and an inactivated myosin were added to actin. The duration of the {"}clearing phase{"} decreased, while the rate and extent of s.p. increased up to a constant value when the myosin fragment concentration was raised. The extent and rate were higher while the delay time shorter for HMM, as compared to S-1 at the same concentration, No s.p. could be detected when: a) an inactivated myosin fragment or the ATPase apyrase was used; b) MgATP was replaced by Mg-pyrophosphate; c) the ability of myosin to form {"}rigor{"} complex with actin has been abolished. It is concluded that the soluble myosin fragment is probably involved in the mechanochemical process associated with s.p..",
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Superprecipitation induced by soluble myosin fragments. / Oplatka, Avraham; Borejdo, Julian; Gadasi, Hanna.

In: Biochemical and Biophysical Research Communications, Vol. 66, No. 4, 27.10.1975, p. 1323-1328.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Superprecipitation induced by soluble myosin fragments

AU - Oplatka, Avraham

AU - Borejdo, Julian

AU - Gadasi, Hanna

PY - 1975/10/27

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N2 - Superprecipitation (s.p.) took place when both an active myosin fragment [heavy meromyosin (HMM) or HMM subfragment-1 (S-1)] and an inactivated myosin were added to actin. The duration of the "clearing phase" decreased, while the rate and extent of s.p. increased up to a constant value when the myosin fragment concentration was raised. The extent and rate were higher while the delay time shorter for HMM, as compared to S-1 at the same concentration, No s.p. could be detected when: a) an inactivated myosin fragment or the ATPase apyrase was used; b) MgATP was replaced by Mg-pyrophosphate; c) the ability of myosin to form "rigor" complex with actin has been abolished. It is concluded that the soluble myosin fragment is probably involved in the mechanochemical process associated with s.p..

AB - Superprecipitation (s.p.) took place when both an active myosin fragment [heavy meromyosin (HMM) or HMM subfragment-1 (S-1)] and an inactivated myosin were added to actin. The duration of the "clearing phase" decreased, while the rate and extent of s.p. increased up to a constant value when the myosin fragment concentration was raised. The extent and rate were higher while the delay time shorter for HMM, as compared to S-1 at the same concentration, No s.p. could be detected when: a) an inactivated myosin fragment or the ATPase apyrase was used; b) MgATP was replaced by Mg-pyrophosphate; c) the ability of myosin to form "rigor" complex with actin has been abolished. It is concluded that the soluble myosin fragment is probably involved in the mechanochemical process associated with s.p..

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