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Immunolocalization of glyceraldehyde-3-phosphate dehydrogenase, hexokinase, and carboxypeptidase Y in yeast cells at the ultrastructural level.
Author(s) -
Evert van Tuinen,
Howard Riezman
Publication year - 1987
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 - 10.1177/35.3.3546482
Subject(s) - immunoelectron microscopy , hexokinase , biochemistry , autolysis (biology) , glyceraldehyde 3 phosphate dehydrogenase , cytoplasm , cell fractionation , dehydrogenase , yeast , carboxypeptidase , glyceraldehyde , microbiology and biotechnology , biology , aldolase a , chemistry , enzyme , glycolysis , antibody , immunology
We have developed a simple and effective method to embed whole yeast cells in Lowicryl resins with excellent ultrastructural and antigenic preservation. Using affinity-purified antibodies eluted from electrophoretically separated proteins transferred to nitrocellulose, we have shown by immunoelectron microscopy that two glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase and hexokinase, are present in the cytoplasm and the nucleus. Carboxypeptidase Y is localized in the yeast vacuole. These results agree with earlier localization studies based on subcellular fractionation.

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