Purification and characterization of the D(-)-lactate dehydrogenase from Leuconostoc lactis

Richard Fitzgerald; Shawn Doonan; Timothy M. Cogan

doi:10.1016/0020-711X(86)90005-4

Purification and characterization of the D(-)-lactate dehydrogenase from Leuconostoc lactis

Richard Fitzgerald, Shawn Doonan, Timothy M. Cogan

Department of Biological Sciences

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

Abstract

1. 1. The d-lactate dehydrogenase from Leuconostoc lactis has been purified in high yield. 2. 2.The enzyme is a dimer of subunits of M_r = 39,000 and each subunit contains a single thiol group. The N-terminal residue is methionine. 3. 3. The amino acid composition has been determined and is typical of that of a soluble globular protein.

Original language	English (Ireland)
Pages (from-to)	31-38
Number of pages	8
Journal	International Journal of Biochemistry
Volume	18
Issue number	1
DOIs	https://doi.org/10.1016/0020-711X(86)90005-4
Publication status	Published - 1986

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@article{26330671ddab41c594306a6b60770d57,

title = "Purification and characterization of the D(-)-lactate dehydrogenase from Leuconostoc lactis",

abstract = "1. 1. The d-lactate dehydrogenase from Leuconostoc lactis has been purified in high yield. 2. 2.The enzyme is a dimer of subunits of Mr = 39,000 and each subunit contains a single thiol group. The N-terminal residue is methionine. 3. 3. The amino acid composition has been determined and is typical of that of a soluble globular protein.",

author = "Richard Fitzgerald and Shawn Doonan and Cogan, \{Timothy M.\}",

year = "1986",

doi = "10.1016/0020-711X(86)90005-4",

language = "English (Ireland)",

volume = "18",

pages = "31--38",

journal = "International Journal of Biochemistry",

issn = "0020-711X",

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T1 - Purification and characterization of the D(-)-lactate dehydrogenase from Leuconostoc lactis

AU - Fitzgerald, Richard

AU - Doonan, Shawn

AU - Cogan, Timothy M.

PY - 1986

Y1 - 1986

N2 - 1. 1. The d-lactate dehydrogenase from Leuconostoc lactis has been purified in high yield. 2. 2.The enzyme is a dimer of subunits of Mr = 39,000 and each subunit contains a single thiol group. The N-terminal residue is methionine. 3. 3. The amino acid composition has been determined and is typical of that of a soluble globular protein.

AB - 1. 1. The d-lactate dehydrogenase from Leuconostoc lactis has been purified in high yield. 2. 2.The enzyme is a dimer of subunits of Mr = 39,000 and each subunit contains a single thiol group. The N-terminal residue is methionine. 3. 3. The amino acid composition has been determined and is typical of that of a soluble globular protein.

UR - https://www.scopus.com/pages/publications/0022630204

U2 - 10.1016/0020-711X(86)90005-4

DO - 10.1016/0020-711X(86)90005-4

M3 - Article

AN - SCOPUS:0022630204

SN - 0020-711X

VL - 18

SP - 31

EP - 38

JO - International Journal of Biochemistry

JF - International Journal of Biochemistry

IS - 1

ER -

Purification and characterization of the D(-)-lactate dehydrogenase from Leuconostoc lactis

Abstract

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