Cytochemical localization of glycoconjugate in mitochondria.
Author(s) -
Richard T. Parmley,
S. S. Spicer,
Kam C. Poon,
Jim A. Wright
Publication year - 1976
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/24.11.1002972
Subject(s) - glycoconjugate , intermembrane space , cytochemistry , mitochondrion , chemistry , biochemistry , inner mitochondrial membrane , horseradish peroxidase , membrane , concanavalin a , biophysics , bacterial outer membrane , microbiology and biotechnology , biology , enzyme , escherichia coli , in vitro , gene
Complex carbohydrates and cations have been localized by cytochemical methods in mitochondria of mammalian leukocytes, hepatocytes and oyster gill epithelium. Glycoconjugate of acidic nature was visualized with the dialyzed iron method in or on the outer membrane and inner boundary membrane and in the outer intermembrane space but not on the membranes of cristae or in the intracristate space, or matrix. Sulfated glycoconjugate was demonstrated with the high iron diamine method in a similar distribution and in, on, or between, membranes of cristae as well. Intermittent aggregates of dialyzed iron and high iron diamine stained material were often found in the outer intermembrane space. The periphery of isolated rat liver mitochondria also stained with a Concanavalin A horseradish peroxidase technique, indicating the presence of macromolecules, presumably glycoproteins containing mannose or glucose. The distribution of antimonate reactive cation in mitochondria of leukocytes resembled that of the acidic glycoconjugate, indicating binding of cations to anionic groups of the latter. The complex carbohydrates and cations demonstrated cytochemically in mitochondria are considered in relation to previous biochemical studies.
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