Die erschöpfende reinigung von aktin-präparaten zahl und art der phosphathaltigen prosthetischen gruppen von G- und F-aktin

Ulbrecht, M.; Grubhofer, N.; Jaisle, F; Walter, S.

doi:10.1016/0006-3002(60)91481-5

Cited by 58 publications

(12 citation statements)

References 19 publications

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“…100000 (obtained from aminoethylated actin, which does not include 3-methylhistidine, analysed by the extended basic amino analysis system), the minimum molecular weight for actin would be 50 000. This value should be compared with the recently published values obtained by the standard physicochemical procedures (Ulbrecht, Grubhofer, Jaisle & Walter, 1960;Adelstein et al 1963;Lewis, Maruyama, Carroll, Kominz & Laki, 1963;Mihashi, 1964;Krans, Van Eijk & Westenbrink, 1965). Although these range from 47 000 to 62 000, most values lie close to 60 000.…”

Section: Discussionmentioning

confidence: 99%

3-Methylhistidine in actin and other muscle proteins

Johnson

Harris

Perry

1967

Biochemical Journal

237

104

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1. By the use of the extended elution system for basic amino acid analysis, 3-methylhistidine has been detected in hydrolysates of actin isolated from mammalian, fish and bird skeletal muscle. 2. Evidence is presented to indicate that 3-methylhistidine forms part of the primary structure and that in rabbit actin this residue is restricted to one peptide fraction obtained from the tryptic digest. 3. Rabbit skeletal-muscle actin has a 3-methylhistidine:histidine ratio 1:7·6, indicating a minimum molecular weight of 47600. 4. Adult rabbit myosin contains approximately 2 3-methylhistidine residues/mol. These residues are localized in the heavy meromyosin part of the molecule, and are restricted to the major component obtained after succinylation.

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Section: Discussionmentioning

confidence: 99%

3-Methylhistidine in actin and other muscle proteins

Johnson

Harris

Perry

1967

Biochemical Journal

237

104

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“…Myosin was prepared from rabbit muscle by the method of Szent-Gyorgyi (1), and actin was prepared according to Ulbrecht et al (10), except that no magnesium was added during the preparation of either protein. The hydrolysis of ATP was recorded by an automatic pH-stat at pH 7.…”

Section: The Contraction Of Skeletal Muscle Depends Upon a Specific Imentioning

confidence: 99%

“…et al(10), except that no magnesium was added during the preparation of either protein. The hydrolysis of ATP was recorded by an automatic pH-stat at pH 7.…”

mentioning

confidence: 99%

Actin-Myosin Interaction: Inhibition of the Myosin Adenosine Triphosphatase by Actin

Barron

Eisenberg

Moos

1966

Science

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“…The actin was prepared from rabbit skeletal muscle dry acetone powder derived from contracted muscle, according CERVI~N to Ulbrecht et al (1960) as described by Drabikowski & Gergely (1962). The powder was extracted for 15 min at 0 ~ C with 2 mM Tris-HC1, pH 7.4 at 0 ~ C, containing 0.2 mM ATP (ATP contributed potassium ions to I raM) and pelleted for 20 min followed by recentrifugation of the Supernatant for 60 min at 30 000 rpm using an RP-42 rotor and a Hitachi 55P-7 preparative ultracentrifuge, to allow for sedimentation of the 0~-actinin.…”

Section: Methodsmentioning

confidence: 99%

Facilitation of actin polymerization by interfilamentous factors

Cervén

1987

J Muscle Res Cell Motil

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The polymerization of actin in low ionic strength buffer at 0 degrees C in the presence of 0.25 mM Mg2+ was studied by viscometry, turbidity and absorbance at 232 nm. Under these conditions, significant polymerization occurred only in the viscometer and not in isotropic mixtures. The polymerization rate with 0.25 mM MgCl2, as judged from shear viscosity, was equal to or greater than that observed with 0.1 M KCl and 0.25 mM MgCl2 at 0 degrees C, and was characterized by a longer nucleation period. Measurements of the turbidity at 350 nm (detecting filament formation and aggregation) and the absorbance at 232 nm (detecting conformational changes of the G-F transition) showed no evidence for polymerization or nucleation in a bulk solution at 0 degrees C when Mg2+ was added to 0.25 mM and, furthermore, F-actin nuclei were ineffective as seeds under these conditions. However, nucleation and polymerization by these criteria could be induced by raising the temperature to 20 degrees C. These results demonstrate the existence of narrow conditions when elongation of F-actin is dissociated from nucleation of oligomeric acceptor nuclei, even if monitored on the sub-molecular level (absorbance at 232 nm). Under these conditions, elongation appears to require anisotropic F-actin, i.e. that filaments are ordered by laminar flow.

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Die erschöpfende reinigung von aktin-präparaten zahl und art der phosphathaltigen prosthetischen gruppen von G- und F-aktin

Cited by 58 publications

References 19 publications

3-Methylhistidine in actin and other muscle proteins

3-Methylhistidine in actin and other muscle proteins

Actin-Myosin Interaction: Inhibition of the Myosin Adenosine Triphosphatase by Actin

Facilitation of actin polymerization by interfilamentous factors

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