Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle.

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Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle. / Rasmussen, Hans N; van Hall, Gerrit; Rasmussen, Ulla F.

I: Journal of Physiology, Bind 541, Nr. Pt 2, 2002, s. 575-80.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Rasmussen, HN, van Hall, G & Rasmussen, UF 2002, 'Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle.', Journal of Physiology, bind 541, nr. Pt 2, s. 575-80.

APA

Rasmussen, H. N., van Hall, G., & Rasmussen, U. F. (2002). Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle. Journal of Physiology, 541(Pt 2), 575-80.

Vancouver

Rasmussen HN, van Hall G, Rasmussen UF. Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle. Journal of Physiology. 2002;541(Pt 2):575-80.

Author

Rasmussen, Hans N ; van Hall, Gerrit ; Rasmussen, Ulla F. / Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle. I: Journal of Physiology. 2002 ; Bind 541, Nr. Pt 2. s. 575-80.

Bibtex

@article{16266530ac0211ddb5e9000ea68e967b,
title = "Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle.",
abstract = "The presence of lactate dehydrogenase in skeletal muscle mitochondria was investigated to clarify whether lactate is a possible substrate for mitochondrial respiration. Mitochondria were prepared from 100 mg samples of human and mouse vastus lateralis muscle. All fractions from the preparation procedure were assayed for marker enzymes and lactate dehydrogenase (LDH). The mitochondrial fraction contained no LDH activity (detection limit approximately 0.05 % of the tissue activity) and the distribution of LDH activity among the fractions paralleled that of pyruvate kinase, i.e. LDH was fractionated as a cytoplasmic enzyme. Respiratory experiments with the mitochondrial fraction also indicated the absence of LDH. Lactate did not cause respiration, nor did it affect the respiration of pyruvate + malate. The major part of the native cytochrome c was retained in the isolated mitochondria, which, furthermore, showed high specific rates of state 3 respiration. This excluded artificial loss from the mitochondria of all activity of a possible LDH. It was concluded that skeletal muscle mitochondria are devoid of LDH and unable to metabolize lactate.",
author = "Rasmussen, {Hans N} and {van Hall}, Gerrit and Rasmussen, {Ulla F}",
note = "Keywords: Animals; Biological Markers; Citrate (si)-Synthase; Cytochrome c Group; Humans; L-Lactate Dehydrogenase; Mice; Mitochondria, Muscle; Muscle, Skeletal; Oxygen Consumption; Pyruvate Kinase; Reproducibility of Results; Species Specificity",
year = "2002",
language = "English",
volume = "541",
pages = "575--80",
journal = "The Journal of Physiology",
issn = "0022-3751",
publisher = "Wiley-Blackwell",
number = "Pt 2",

}

RIS

TY - JOUR

T1 - Lactate dehydrogenase is not a mitochondrial enzyme in human and mouse vastus lateralis muscle.

AU - Rasmussen, Hans N

AU - van Hall, Gerrit

AU - Rasmussen, Ulla F

N1 - Keywords: Animals; Biological Markers; Citrate (si)-Synthase; Cytochrome c Group; Humans; L-Lactate Dehydrogenase; Mice; Mitochondria, Muscle; Muscle, Skeletal; Oxygen Consumption; Pyruvate Kinase; Reproducibility of Results; Species Specificity

PY - 2002

Y1 - 2002

N2 - The presence of lactate dehydrogenase in skeletal muscle mitochondria was investigated to clarify whether lactate is a possible substrate for mitochondrial respiration. Mitochondria were prepared from 100 mg samples of human and mouse vastus lateralis muscle. All fractions from the preparation procedure were assayed for marker enzymes and lactate dehydrogenase (LDH). The mitochondrial fraction contained no LDH activity (detection limit approximately 0.05 % of the tissue activity) and the distribution of LDH activity among the fractions paralleled that of pyruvate kinase, i.e. LDH was fractionated as a cytoplasmic enzyme. Respiratory experiments with the mitochondrial fraction also indicated the absence of LDH. Lactate did not cause respiration, nor did it affect the respiration of pyruvate + malate. The major part of the native cytochrome c was retained in the isolated mitochondria, which, furthermore, showed high specific rates of state 3 respiration. This excluded artificial loss from the mitochondria of all activity of a possible LDH. It was concluded that skeletal muscle mitochondria are devoid of LDH and unable to metabolize lactate.

AB - The presence of lactate dehydrogenase in skeletal muscle mitochondria was investigated to clarify whether lactate is a possible substrate for mitochondrial respiration. Mitochondria were prepared from 100 mg samples of human and mouse vastus lateralis muscle. All fractions from the preparation procedure were assayed for marker enzymes and lactate dehydrogenase (LDH). The mitochondrial fraction contained no LDH activity (detection limit approximately 0.05 % of the tissue activity) and the distribution of LDH activity among the fractions paralleled that of pyruvate kinase, i.e. LDH was fractionated as a cytoplasmic enzyme. Respiratory experiments with the mitochondrial fraction also indicated the absence of LDH. Lactate did not cause respiration, nor did it affect the respiration of pyruvate + malate. The major part of the native cytochrome c was retained in the isolated mitochondria, which, furthermore, showed high specific rates of state 3 respiration. This excluded artificial loss from the mitochondria of all activity of a possible LDH. It was concluded that skeletal muscle mitochondria are devoid of LDH and unable to metabolize lactate.

M3 - Journal article

C2 - 12042361

VL - 541

SP - 575

EP - 580

JO - The Journal of Physiology

JF - The Journal of Physiology

SN - 0022-3751

IS - Pt 2

ER -

ID: 8442703