Immunoelectron microscopic localization of carbonic anhydrase III in rat skeletal muscle
- 1 January 1986
- journal article
- research article
- Published by Springer Nature in Histochemistry and Cell Biology
- Vol. 86 (2) , 175-179
- https://doi.org/10.1007/bf00493384
Abstract
The subcellular distribution of carbonic anhydrase III in rat soleus and vastus lateralis muscles was studied using an immunogold technique. The enzyme protein was found to be distributed diffusely in the cytoplasm of skeletal muscle cells. Red skeletal muscle (mainly type I fibers) revealed very strong immunogold staining whereas in white muscle (mainly type II fibers) gold particles were almost completely absent. No immunoreaction was observed in mitochondria or in other intracellular organelles.Keywords
This publication has 17 references indexed in Scilit:
- Purification and localization of human carbonic anhydraseHistochemistry and Cell Biology, 1985
- Specific arginine modification at the phosphatase site of muscle carbonic anhydraseBiochemistry, 1985
- Rapid embedding of tissues in Lowicryl K4M for immunoelectron microscopy.Journal of Histochemistry & Cytochemistry, 1984
- Origins and Molecular Evolution of the Carbonic Anhydrase IsozymesaAnnals of the New York Academy of Sciences, 1984
- Hormonal Control of Carbonic Anhydrase IIIAnnals of the New York Academy of Sciences, 1984
- Carbonic anhydrase-III immunohistochemical localization in human skeletal muscleActa Neuropathologica, 1983
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Purification, Molecular Properties and Ontogeny of Carbonic Anhydrase Isozymes. Evidence for A, B and C Isozymes in Avian and Mammalian TissuesEuropean Journal of Biochemistry, 1977
- Basic muscle protein, a third genetic locus isoenzyme of carbonic anhydrase?Biochemical and Biophysical Research Communications, 1977
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970