Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle.

Histochemistry ·Vol. 52 ·No. 3 ·1977-06-08 ·Pages 201-16

Spamer C, Pette D

Abstract

Methods for standardized determination of phosphofructokinase (PFK), glyceraldehydephosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH) and malate dehydrogenase (MDH) activities in nanogram samples of microdissected single fibres of rabbit psoas and soleus muscle are described. Fast and slow fibres in soleus muscle show lower absolute activities of these enzymes than the respective fibre types in psoas muscle. Slow fibres represent a more uniform population in the two muscles according to absolute and relative activities of the enzymes investigated. Slow fibres are characterized by high activities of MDH and relatively low activities of glycolytic enzymes. Fast fibres in the soleus muscle represent a population with high activities of MDH and glycolytic enzymes. Fast fibres in psoas muscle represent a heterogeneous population with high activities of glycolytic enzymes and extremely variable activity of MDH. More than 10-fold differences exist in the MDH activities of the extreme types of this fibre population. Differences in the activity levels of MDH in single fast type fibres but also in the activities of glycolytic enzymes between fast and slow fibres are greater than those reported between extreme white and red rabbit muscles.

MeSH Terms

Animals Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism Glycolysis L-Lactate Dehydrogenase/metabolism Malate Dehydrogenase/metabolism Male Muscles/enzymology Phosphofructokinase-1/metabolism Rabbits

Chemicals

L-Lactate Dehydrogenase Malate Dehydrogenase Glyceraldehyde-3-Phosphate Dehydrogenases Phosphofructokinase-1

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Spamer C

Pette D

References (25)

25 references, click to expand

Metabolic characteristics of fibre types in human skeletal muscle.
Acta Physiol Scand. 1975 Oct;95(2):153-65 PMID: 242187
Dynamic properties of mammalian skeletal muscles.
Physiol Rev. 1972 Jan;52(1):129-97 PMID: 4256989
The specificity of the histochemical method for adenosine triphosphatase.
J Histochem Cytochem. 1955 May;3(3):170-95 PMID: 14381606
[Proportionally constant groups in relation to the differentiation of enzyme activity patterns of skeletal muscles in rabbits].
Hoppe Seylers Z Physiol Chem. 1963 Mar;331:180-95 PMID: 13942962
Temporal progress of muscle adaptation to endurance training in hind limb muscles of young rats. A histochemical and morphometrical study.
Cell Tissue Res. 1974;156(1):61-87 PMID: 4281715
Microphotometric determination of enzyme activity in single cells in cryostat section. II. Succinate dehydrogenase, lactate dehydrogenase and triosephosphate dehydrogenase activities in red, intermediate and white fibers of soleus and rectus femoris muscles of rat.
J Histochem Cytochem. 1972 Aug;20(8):577-82 PMID: 5044279
Some aspects of regulation of enzyme levels in muscle energy-supplying metabolism.
Adv Enzyme Regul. 1975;13:355-77 PMID: 128997
ATPase activity of myosin correlated with speed of muscle shortening.
J Gen Physiol. 1967 Jul;50(6):Suppl:197-218 PMID: 4227924
Metabolic profiles of three fiber types of skeletal muscle in guinea pigs and rabbits.
Biochemistry. 1972 Jul 4;11(14):2627-33 PMID: 4261555
ENZYMES IN MUSCLES. II. HISTOCHEMICAL AND QUANTITATIVE STUDIES.
Arch Neurol. 1964 Oct;11:369-78 PMID: 14196729
Chemical changes in skeletal muscle during development.
Biochem J. 1960 Feb;74:247-57 PMID: 13816591
Quantitative histochemical analysis of glycolytic intermediates and cofactors with an oil well technique.
J Histochem Cytochem. 1968 Jan;16(1):29-39 PMID: 4296361
The analysis of skeletal muscle by quantitative histochemical techniques.
J Neuropathol Exp Neurol. 1973 Jul;32(3):371-9 PMID: 4125112
An electrophoretic study of the low-molecular-weight components of myosin.
Biochem J. 1970 Aug;119(1):31-8 PMID: 5485752
Histochemical composition, distribution of fibres and fatiguability of single motor units. Anterior tibial muscle of the rat.
J Neurol Neurosurg Psychiatry. 1968 Oct;31(5):424-33 PMID: 5709826
Metabolic differentiation of distinct muscle types at the level of enzymatic organization.
Eur J Biochem. 1969 Sep;10(2):198-206 PMID: 4309865
Effects of long-term electrical stimulation on some contractile and metabolic characteristics of fast rabbit muscles.
Pflugers Arch. 1973 Feb 6;338(3):257-72 PMID: 4736724
The effects of different patterns of muscle activity on capillary density, mechanical properties and structure of slow and fast rabbit muscles.
Pflugers Arch. 1976 Feb 24;361(3):241-50 PMID: 943767
Light chains from fast and slow muscle myosins.
Nature. 1971 Nov 12;234(5324):81-5 PMID: 4942892
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
Histochemical, biochemical, and contractile properties of red, white, and intermediate fibers.
Am J Physiol. 1971 Feb;220(2):410-4 PMID: 4250606
RELATIONS BETWEEN STRUCTURE AND FUNCTION IN THE DESIGN OF SKELETAL MUSCLES.
J Neurophysiol. 1965 May;28:581-98 PMID: 14328455
Histochemical characteristics of vertebrate striated muscle: a review.
Prog Histochem Cytochem. 1976;8(4):1-48 PMID: 185661
Differences between slow and fast muscle myosin. Adenosine triphosphatase activity and release of associated proteins by p-chloromercuriphenylsulfonate.
J Biol Chem. 1970 Jan 25;245(2):219-24 PMID: 4243949
Light chains of myosins from white, red, and cardiac muscles.
Proc Natl Acad Sci U S A. 1971 May;68(5):946-50 PMID: 4252540

Article Info

Journal

Histochemistry

Abbr.

Histochemistry

ISSN

0301-5564

DOI

10.1007/BF00495857

Published

1977-06-08

Pages

201-16

Language

English

Region

Germany

NLM ID

0411300

Subset

External Links

PubMed source DOI: 10.1007/BF00495857

Analysis Services

Activity patterns of phosphofructokinase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase and malate dehydrogenase in microdissected fast and slow fibres from rabbit psoas and soleus muscle.

Contact

WeChat Official Account