A study of the binding of adenosine diphosphate to myosin subfragment-1.

A study of the binding of adenosine diphosphate to myosin subfragment-1. Research Abstract Details 

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A study of the binding of adenosine diphosphate to myosin subfragment-1. Abstract Text:

M Yoshida,F Morita,

The binding of ADP to subfragment-1 was investigated by the gel filtration method. The amount of bound ADP was determined as a function of free ADP concentration. Linear Scatchard plots were obtained. The maximum binding number, 0.55 mole of ADP per 10(5) g of protein, and the dissociation constant, 1.6 x 10(-6) M, were obtained, using subfragment-1 prepared by tryptic digestion, in the presence of 0.083 M KCl-10 mM MgCl2-0.02 M Tris-HCl (pH 8), at 25 degrees. Similar maximum numbers, about 0.5 mole per 10(5) g of protein, were obtained with subfragment-1 prepared by chymotryptic digestion of myosin or papain digestion of myofibrils. The maximum number did not depend on the KCl concentration or the temperature, while the dissociation constant decreased on decreasing either the KCl concentration or the temperature. Adenylyl imidodiphosphate binding to subfragment-1 prepared by chymotryptic digestion was also measured by the gel filtration method. The maximum binding number, 0.41 mole per 10(5) g of subfragment-1, and the dissociation constant, less than 10(-7) M, were obtained in the presence of 0.7 M KCl-10 mM MgCl2-0.02 M Tris-HCl (pH 8), at 8 degrees. The difference absorbance at 288 nm of the difference absorption spectrum induced by ADP of subfragment-1 prepared by tryptic digestion was proportional to the amount of bound ADP. The steady-state ATPase rate of subfragment-1 prepared by tryptic digestion was inhibited competitively by ADP in the presence of MgCl2. The extent of the initial burst of ATPase [EC 3.6.1.3] decreased from 0.46 +/- 0.06 to 0.30 +/- 0.09 mole of Pi per 10(5) g of subfragment-1 on adding ADP to a level of 0.6 mM. Subfragment-1 prepared by tryptic digestion bound F-actin with a mole ratio of 1/0.96 of actin monomer. The binding was depressed by the addition of ADP. On the basis of these results, subfragment-1 preparations were assumed to be a half-and-half mixture of two kinds of protein, and properties of each protein are discussed.

A study of the binding of adenosine diphosphate to myosin subfragment-1. Publishing Authors By Initials

M Yoshida,F Morita,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

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A study of the binding of adenosine diphosphate to myosin subfragment-1. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 77

Page Numbers: 983-92

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: May

YEAR: 1975

A study of the binding of adenosine diphosphate to myosin subfragment-1. Information

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LANGUAGE: eng

NlmUniqueID: 376600

A study of the binding of adenosine diphosphate to myosin subfragment-1. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: pharmacology

Chemical & Substance for Abstract: A study of the binding of adenosine diphosphate to myosin subfragment-1. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

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Country: JAPAN

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MEDLINETA: J Biochem

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