Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1.

Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1. Research Abstract Details 

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Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1. Abstract Text:

Shinsaku Maruta,Yoshiaki Mizukura,Shigeru Chaen,

A new fluorescent ribose-modified ATP analogue, 2'(3')-O-[6-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoic]-ATP (NBD-ATP), was synthesized and its interaction with skeletal muscle myosin subfragment-1 (S-1) was studied. NBD-ATP was hydrolysed by S-1 at a rate and with divalent cation-dependence similar to those in the case of regular ATP. Skeletal HMM supported actin translocation using NBD-ATP and the velocity was slightly higher than that in the case of regular ATP. The addition of S1 to NBD-ATP resulted in quenching of NBD fluorescence. Recovery of the fluorescence intensity was noted after complete hydrolysis of NBD-ATP to NBD-ADP. The quenching of NBD-ATP fluorescence was accompanied by enhancement of intrinsic tryptophan fluorescence. These results suggested that the quenching of NBD-ATP fluorescence reflected the formation of transient states of ATPase. The formation of S-1.NBD-ADP.BeF(n) and S-1.NBD-ADP.AlF(4)(-) complexes was monitored by following changes in NBD fluorescence. The time-course of the formation fitted an exponential profile yielding rate constants of 7.38 x 10(-2) s(-1) for BeF(n) and 1.1 x 10(-3) s(-1) for AlF(4)(-). These values were similar to those estimated from the intrinsic fluorescence enhancement of trp due to the formation of S-1.ADP.BeF(n) or AlF(4)(-) reported previously by our group. Our novel ATP analogue seems to be applicable to kinetic studies on myosin.

Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1. Publishing Authors By Initials

S Maruta,Y Mizukura,S Chaen,

For similar macromolecular substances: polymers: biopolymers: microfilament proteins: myosins: myosin subfragments research abstracts see: macromolecular substances: polymers: biopolymers: microfilament proteins: myosins: myosin subfragments research

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Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 131

Page Numbers: 905-11

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jun

YEAR: 2002

Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1. Keywords Mesh Terms:

KEYWORDS: Myosin Subfragments

MESH TERMS: metabolism

Chemical & Substance for Abstract: Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1. Information

Substance Name: Adenosine Diphosphate

Registry Number: 58-64-0

Grant and Affiliation Information for Interaction of a new fluorescent ATP analogue with skeletal muscle myosin subfragment-1.

AFFILIATION: Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan. shinsaku@t.soka.ac.jp

Country: Japan

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MEDLINETA: J Biochem

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