Primary structure of the essential thiol peptide from the lactate dehydrogenase C subunit

Thomas E. Wheat; Erwin Goldberg; E. Margoliash

doi:10.1016/0006-291X(77)91626-6

Primary structure of the essential thiol peptide from the lactate dehydrogenase C subunit

Thomas E. Wheat^*, Erwin Goldberg, E. Margoliash

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Lactate dehydrogenase isozymes are inhibited when mercurial reagents are bound to cysteine-165 although no functional role is ascribed to this residue. Identical tryptic peptides containing this cysteine have been isolated from many LDH isozymes, including both A and B subunits. This report identifies an identical peptide from a third subunit type, C, of mouse. The rigorous conservation of this sequence implies an important functional role for this region of the molecule.

Original language	English (US)
Pages (from-to)	1066-1070
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	74
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(77)91626-6
State	Published - Feb 7 1977

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Primary structure of the essential thiol peptide from the lactate dehydrogenase C subunit",

abstract = "Lactate dehydrogenase isozymes are inhibited when mercurial reagents are bound to cysteine-165 although no functional role is ascribed to this residue. Identical tryptic peptides containing this cysteine have been isolated from many LDH isozymes, including both A and B subunits. This report identifies an identical peptide from a third subunit type, C, of mouse. The rigorous conservation of this sequence implies an important functional role for this region of the molecule.",

author = "Wheat, {Thomas E.} and Erwin Goldberg and E. Margoliash",

note = "Funding Information: ACKNOWLEDGEMENTS: Automated Edman degradations were performed with the assistance of Drs. James Beecher and George Tarr. Amino acid analyses performed with the support of NIH grant No. HL-11119. This research supported by NIH grant No. ROl HD05863. We appreciate the helpful of Dr. S.S. Taylor and editorial assistance by P. Bentley. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.",

year = "1977",

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doi = "10.1016/0006-291X(77)91626-6",

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T1 - Primary structure of the essential thiol peptide from the lactate dehydrogenase C subunit

AU - Wheat, Thomas E.

AU - Goldberg, Erwin

AU - Margoliash, E.

N1 - Funding Information: ACKNOWLEDGEMENTS: Automated Edman degradations were performed with the assistance of Drs. James Beecher and George Tarr. Amino acid analyses performed with the support of NIH grant No. HL-11119. This research supported by NIH grant No. ROl HD05863. We appreciate the helpful of Dr. S.S. Taylor and editorial assistance by P. Bentley. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1977/2/7

Y1 - 1977/2/7

N2 - Lactate dehydrogenase isozymes are inhibited when mercurial reagents are bound to cysteine-165 although no functional role is ascribed to this residue. Identical tryptic peptides containing this cysteine have been isolated from many LDH isozymes, including both A and B subunits. This report identifies an identical peptide from a third subunit type, C, of mouse. The rigorous conservation of this sequence implies an important functional role for this region of the molecule.

AB - Lactate dehydrogenase isozymes are inhibited when mercurial reagents are bound to cysteine-165 although no functional role is ascribed to this residue. Identical tryptic peptides containing this cysteine have been isolated from many LDH isozymes, including both A and B subunits. This report identifies an identical peptide from a third subunit type, C, of mouse. The rigorous conservation of this sequence implies an important functional role for this region of the molecule.

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Primary structure of the essential thiol peptide from the lactate dehydrogenase C subunit

Abstract

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