Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1.

Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. Research Abstract Details 

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Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. Abstract Text:

S Kunori,T Katoh,Y Mogi,F Morita,

The N-terminal 28-residue peptide of actin whose Cys10 was labeled with 5-iodoacetamido-fluorescein (F3K peptide) was isolated from the fluorescently labeled thrombin digest of actin. The effect of myosin subfragment 1 (S1) on the fluorescence of F3K peptide was examined in the absence of ATP. With increasing concentration of S1 added, the fluorescence intensity of F3K peptide increased by maximally 7.3% with an apparent dissociation constant of 5.7 microM, suggesting a role of this peptide region of actin in acto-S1 binding in rigor. F3K peptide was crosslinked with S1 at 10 mM NaCl using a zero-length crosslinker by the method of Grabarek and Gergely [Anal. Biochem. 185, 131-135 (1990)]. The crosslinking was greatly inhibited by the presence of either 0.2 M NaCl or 5 mM MgATP. The analyses of amino acid compositions and sequences of the fluorescent peptides isolated from a lysylendopeptidase digest of the crosslinked S1 indicated that F3K peptide was mainly crosslinked to residues 637-642 of the S1 heavy chain. The crosslinked S1 was isolated by selectively pelleting the uncrosslinked S1 with F-actin. ATPase activity of the isolated crosslinked S1 alone was twice as high as that of control S1. The actin-activated ATPase activity of the crosslinked S1 was much lower than that of uncrosslinked S1. The estimated Vm and Km values were 1.72 s-1 and 125 microM, respectively. The Vm decreased to less than 1/8, while Km increased only twofold. The results suggest that the N-terminal 28-residue segment of actin may be implicated in the rigor binding of actomyosin and in the actin-activation of myosin ATPase, but may not be the main determinant of actomyosin binding in the presence of ATP.

Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. Publishing Authors By Initials

S Kunori,T Katoh,Y Mogi,F Morita,

For similar investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research abstracts see: investigative techniques: chemistry, analytical: photometry: luminescent measurements: fluorometry: spectrometry, fluorescence research

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Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 118

Page Numbers: 1239-47

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1995

Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. Keywords Mesh Terms:

KEYWORDS: Spectrometry, Fluorescence

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1. Information

Substance Name: Endopeptidases

Registry Number: EC 3.4.-

Grant and Affiliation Information for Crosslinking of a 28-residue N-terminal peptide of actin to myosin subfragment 1.

AFFILIATION: Department of Chemistry, Hokkaido University, Sapporo.

Country: JAPAN

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MEDLINETA: J Biochem

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