Abstract
The study of cellular organelles, while a collaborative effort, usually begins with the morphological observations of the cell anatomist followed by the biochemist’s analysis of the isolated organelles and their molecular components. The pattern was reversed for lysosomes, the nature and function of which were not recognized until they had been characterized chemically. The discovery of lysosomes began in 1949 by Dr. Christian de Duve and his colleagues, with an investigation of rat liver enzymes involved in carbohydrate metabolism. Using the then newly developed technique of centrifugal fractionation of cells, a class of subcellular particles having centrifugal properties intermediate between those of mitochondria and microsomes was isolated. These were found to have a high content of acid phosphatase and other hydrolytic enzymes. By centrifugation, it was calculated that the size of the particles was 0.2–0.8 μ. It was also determined that these enzymes were inactive towards their potential substrates if the fraction was carefully prepared to avoid disruption of the organelles. However, preparation of the fraction without regard to cellular organization, or exposure of the fraction to decreased osmotic pressure or surface active agents, resulted in a considerable increase in enzyme activity (De Duve et al., 1949; De Duve, 1959, 1965). This special relationship between particle and enzymes whereby disruption of the organelle is required for maximum enzyme activity is termed “structure-linked latency” and its establishment led to the hypothesis that the acid hydrolases were packaged together in a previously undescribed, membrane-bounded organelle.
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Zurier, R.B., Krakauer, K. (1978). Lysosomal Enzymes. In: Vane, J.R., Ferreira, S.H. (eds) Inflammation. Handbook of Experimental Pharmacology, vol 50 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-66888-3_10
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DOI: https://doi.org/10.1007/978-3-642-66888-3_10
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