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Differences between the endocytosis of horseradish peroxidase and its conjugate with wheat germ agglutinin by cultured fibroblasts
Author(s) -
Stieber Anna,
Gonatas Jacqueline O.,
Gonatas Nicholas K.
Publication year - 1984
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041190112
Subject(s) - conjugate , horseradish peroxidase , endocytosis , wheat germ agglutinin , vesicle , peroxidase , agglutinin , golgi apparatus , chemistry , endosome , biochemistry , biology , membrane , enzyme , intracellular , endoplasmic reticulum , lectin , cell , mathematical analysis , mathematics
A covalent conjugate of wheat germ agglutinin (WGA) with horseradish peroxidase (HRP) was used for a morphologic study of its adsorptive endocytosis by cultured human fibroblasts. Initial binding at 4°C of the conjugate was observed over the entire plasma membrane, including “coated” and smooth pits. Endocytosis of HRP and the WGA‐HRP conjugate was observed in lysosomes, but only the conjugate was seen in a cisterna of the Golgi apparatus (GERL), and in adjacent coated vesicles.