Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue.

Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue. Research Abstract Details 

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Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue. Abstract Text:

F Morita,A Matsumoto,

Binding of divalent metal ions to the g1 subunit isolated from myosin was shown by the difference UV-absorption spectrum. The difference spectrum indicated movement of a tyrosyl residue of g1. The residue responsible for the difference spectrum was assigned to be 180 Tyr.

Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue. Publishing Authors By Initials

F Morita,A Matsumoto,

For similar amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, cyclic: amino acids, aromatic: tyrosine research

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Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue. Journal Published:

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

Journal: Journal of biochemistry

VOLUME: 88

Page Numbers: 1883-6

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1980

Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue. Keywords Mesh Terms:

KEYWORDS: Tyrosine

MESH TERMS: metabolism

Chemical & Substance for Abstract: Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue. Information

Substance Name: Myosins

Registry Number: EC 3.6.1.4

Grant and Affiliation Information for Divalent metal ion binding to g1 subunit of myosin and movement of 180 tyrosyl residue.

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Country: JAPAN

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MEDLINETA: J Biochem

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