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

8 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

Funding

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.

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
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",

month = feb,

day = "7",

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

language = "English (US)",

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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

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