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PMID: 14195619 Published · ppublish English Journal Article

CYTOCHEMICAL LOCALIZATION OF LACTIC DEHYDROGENASE IN WHITE SKELETAL MUSCLE.

The Journal of cell biology ·Vol. 22 ·1964-07-00 ·Pages 29-48

FAHIMI HD, AMARASINGHAM CR

Abstract

The limitations of the conventional histochemical methods for localization of lactic dehydrogenase (LDH) in white skeletal muscle have been analyzed quantitatively. It is demonstrated that more than 80 per cent of LDH diffuses into the incubation medium within the first 10 minutes of incubation. Furthermore, it is confirmed that the addition of phenazine methosulfate (PMS) to the ingredients of the histochemical reaction for LDH increases substantially the capacity of the white muscle extract to reduce Nitro-BT. Based on these observations, a modified method of cytochemical localization of LDH has been developed. This method prevents the leakage of LDH from tissue sections by the application of all the ingredients of the histochemical reaction to tissue sections in a thin gelatin film. The incubation mixture contains PMS so that the staining system is independent of tissue diaphorase. The application of this method to the adductor magnus muscle of the rabbit revealed a fine reticulum in the sarcoplasm of all muscle fibers, in addition to the staining of mitochondria. The distribution of the staining suggests that LDH is localized in the sarcoplasmic reticulum.

Keywords
EXPERIMENTAL LAB STUDY HISTOCYTOCHEMISTRY LACTATE DEHYDROGENASE MUSCLES RABBITS
MeSH Terms
Animals Histocytochemistry L-Lactate Dehydrogenase Muscle, Skeletal Muscles Oxidoreductases Rabbits Research Sarcoplasmic Reticulum Staining and Labeling
Chemicals
Oxidoreductases L-Lactate Dehydrogenase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
FAHIMI H D
AMARASINGHAM C R
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47 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.22.1.29
Published
1964-07-00
Pages
29-48
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2106480
Subset
OM
External Links
PubMed source DOI: 10.1083/jcb.22.1.29 PMC Full Text View journal details
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