Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Interaction of actin and myosin in the absence and presence of ATP

Dancker, P., & Hoffmann, M. (1973). Interaction of actin and myosin in the absence and presence of ATP. Zeitschrift für Naturforschung, C: Journal of Biosciences, 28(7-8), 401-421. doi:10.1515/znc-1973-7-808.

Item is

Basisdaten

einblenden: ausblenden:
Genre: Zeitschriftenartikel

Dateien

einblenden: Dateien
ausblenden: Dateien
:
ZsNaturforschC_28_1973_401.pdf (beliebiger Volltext), 12MB
 
Datei-Permalink:
-
Name:
ZsNaturforschC_28_1973_401.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Eingeschränkt (Max Planck Institute for Medical Research, MHMF; )
MIME-Typ / Prüfsumme:
application/pdf
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-
Lizenz:
-

Externe Referenzen

einblenden:
ausblenden:
Beschreibung:
-
OA-Status:
externe Referenz:
https://doi.org/10.1515/znc-1973-7-808 (beliebiger Volltext)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Dancker, Peter1, Autor           
Hoffmann, Marianne1, Autor           
Affiliations:
1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

Inhalt

einblenden:
ausblenden:
Schlagwörter: -
 Zusammenfassung: The binding between F-actin and myosin has been studied by analyzing the amount of radio-actively labelled (by means of 14C-NEM) F-actin and myosin in the formed unsoluble actomyosin pellet after centrifugation of the reaction mixture. In the absence of ATP, the amount of actin bound to myosin varies, depending on the amounts of actin and myosin present, between 0.18 mg actin/mg myosin (2 actin units per 1 myosin molecule) and about 2 mg actin/mg myosin (each actin fibril only uncompletely saturated with myosin). In 0.03 ᴍ KCl ATP decreases, if at all, the affinity of actin towards myosin only slightly; but less actin is bound to myosin in the presence of MgATP and in low ionic strength, indicating that myosin is now more densily distributed over fewer actin fibrils leaving the rest of fibrils free. For precipitation of the total amount of myosin (myosin alone is soluble in MgATP) incomplete saturation of myosin with actin suffices; obviously actin promotes filament formation of myosin. The activation of myosin ATPase by actin depends in a similar manner as actin binding does on actin concentration, hence the enzymatic interaction between actin and myosin is accompanied by true actin-myosin binding. An actin-tropomyosin-troponin preparation, whose reduced viscosity is lower than that of F-actin and which consists of about 30% actin, activates myosin ATPase to the same extent as F-actin does. It competes with F-actin for the same binding sites on myosin and can in the presence of MgATP be displaced from myosin by those preparations of F-actin which have a strong tendency to become fully saturated with myosin. The activation of myosin ATPase by actin-tropomyosin-troponin is reduced after tryptic digestion of actin-tropomyosin-troponin, which affects, according to SDS gel electro­ phoresis, mainly two components of troponin with molecular weights of about 32 000 and 25 000, respectively.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 1973-04-242014-06-021973-08
 Publikationsstatus: Erschienen
 Seiten: 14
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1515/znc-1973-7-808
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Zeitschrift für Naturforschung, C: Journal of Biosciences
  Kurztitel : Z. Naturforsch., C: J. Biosci.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Berlin : Walter de Gruyter GmbH
Seiten: - Band / Heft: 28 (7-8) Artikelnummer: - Start- / Endseite: 401 - 421 Identifikator: ISSN: 1865-7125
CoNE: https://pure.mpg.de/cone/journals/resource/954927655916_1