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An acid hydrolase is an enzyme that catalyses hydrolysis most effectively under acidic conditions; lysosomes contain multiple kinds.

The lysosomal lumen is the aqueous interior of a lysosome, separated from cytosol by its surrounding lipid bilayer. A membrane pump couples ATP hydrolysis to inward transport of hydrogen ions, maintaining an acidic environment for acid hydrolases. Membrane transport proteins export digestion products, including amino acids and sugars, for reuse in metabolism. Compartmentalization combines restricted access with controlled exchange.^[ref]

A lysosome is an acidic digestive and recycling organelle: one surrounding lipid bilayer encloses a lysosomal lumen containing acid hydrolases. These enzymes break down proteins, nucleic acids, carbohydrates and lipids by hydrolysis. Cargo can originate outside the biological cell, entering through endocytosis, or within its own cytoplasm, delivered through autophagy. Digestion therefore serves both disposal and reuse.^[ref]

An endosome sorts endocytosed cargo: some returns to the cell membrane, while some proceeds toward lysosomes. An autophagosome instead encloses material already in the cytoplasm. Both routes bring cargo into contact with digestive enzymes; neither implies that every internalized molecule is destroyed.^[ref]

Enzyme supply is a different itinerary from cargo disposal. Secretory protein routing and protein targeting deliver newly made digestive enzymes through the endoplasmic reticulum, Golgi apparatus and trans-Golgi network toward lysosomes.^[ref] The existing membrane transport and differential centrifugation articles explain the boundary-crossing and separation principles used below.

A proteasome is a different digestive machine: a protein complex without a surrounding lipid bilayer, acting on individual proteins in the cytosol and cell nucleus. Many targets carry ubiquitin chains. A lysosome accepts a much broader range of cargo, including material delivered inside an autophagosome. Thus an unwanted soluble protein and an unwanted mitochondrion pose different disposal problems; a proteasome does not swallow an intact mitochondrion.^[ref]

In the 1951 study by Jacques Berthet and Christian de Duve, liver from fasted rats was immediately chilled in an ice-cold isotonic chemical solution. The tissue was generally pressed through wire mesh; the weighed pulp was homogenized in cold $0.25\mathrm{mol}{\mathrm{L}}^{-1}$ sucrose using a glass Potter-Elvehjem homogenizer. Their acid phosphatase test concerned activity toward added glycerophosphate at pH $5$: the readout was substrate hydrolysis, rather than an image of a particle.^[ref]

Christian de Duve's retrospective describes successive centrifugation steps, separating centrifugation pellets and supernatants, and comparing enzyme distributions across the recovered fractions. Membrane disruption exposed previously inaccessible acid phosphatase activity, providing the crucial comparison with the membrane-preserving preparation. Joint fractionation patterns and release behavior of several acid hydrolases supported a shared population of digestive particles. By 1955, this evidence supported the lysosome concept.^[ref]

The inference was biochemical: a barrier restricted access to active enzymes. Co-sedimentation could confuse distinct particles; a crude mitochondrial fraction did not establish residence inside mitochondria. Lysosomal enzyme latency neither images an organelle nor determines its shape. Electron microscopy of enriched fractions supplied separate morphological evidence.^[ref]