descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1971 English Publisher:Elsevier BVJournal:Immunochemistry, volume 8, pages 89-97 (issn: 0019-2791,

Authors: V, Gheţie; C, Motaş;

doi: 10.1016/0019-2791(71)90424-1

pmid: 5547695

Catabolism of rabbit immunoglobulin G by some cathepsin-rich subcellular fractions isolated from rat liver

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Abstract

Abstract Lysosomal and mitochondrial fractions of rat liver display a high proteolytic activity because cell cathepsin activity is prevailingly concentrated at this level. By incubating rabbit IgG with these two fractions. Fab-like, Fc-like and Fc′-like fragments were obtained. The number and type of resulting fragments were dependent on the subcelluar fraction used, the pH of hydrolysis and the presence or absence of cysteine. At pH 3.5, in the presence of cysteine. Fc fragment was split to Fc′ fragment and to some TCA-soluble products. Fab fragment could not be digested even in the presence of some energy donors as CoA + ATP.

Related Organizations

Institute of Biochemistry
Romania

Keywords

Immunoglobulins, Mitochondria, Liver, Hydrogen-Ion Concentration, In Vitro Techniques, Cathepsins, Rats, Adenosine Triphosphate, Liver, Solubility, Immunoglobulin G, Iodine Isotopes, Chromatography, Gel, Animals, Coenzyme A, Cysteine, Rabbits, Trichloroacetic Acid, Lysosomes, Immunoelectrophoresis

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