@article{7d8a3c0d90ec4cbca3f5f1ac97d08785,
title = "Subcellular localization of acid hydrolases in rat lungs",
abstract = "The subcellular distribution of twelve acid hydrolases was studied in rat lung homogenates. The distribution profile of all the hydrolases, except cathepsin C (EC 3.4.4.9), is similar to that of lysosomal enzymes in rat and guinea pig liver. The microsomal marker, glucose-6-phosphatase (D-glucose-6-phosphate phosphohydrolase, EC 3.1.3.9), and mitochondrial marker, the succinate oxidase system, were localized mainly in their respective fractions. The increases of specific activities of the light-mitochondrial fraction over the homogenate specific activities are similar to those obtained for rat liver and indicates the usefulness of the differential centrifugation method described for preparation of acid hydrolase-rich fractions from lung homogenates. This study also shows some qualitative similarities in the hydrolase complements of lung and liver.",
author = "{De Lumen}, {B. O.} and S. Taylor and N. Urribarri and Tappel, {A. L.}",
note = "Funding Information: evidence shows a high amount of acid phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.2) in the alveolar macrophages and less in the Type II epithelial cell 16-~s . The peculiar distribution of cathepsin C may indicate that its lysosomal source belongs to a cell type different from that of the other hydrolases. The typically lysosomal distribution of the hydrolases and the several-fold increase of the activities over the homogenate indicate the suitability of using the differential centrifugation employed in this study to prepare subcellular fractions from rat lungs rich in acid hydrolases. This study also reveals the qualitative similarities in the hydrolase complement of rat lung with liver, although they may differ in quantities. This research was supported in part by U.S. Public Health Service Grant ES 00628 and in part by California Air Resources Board Project 7-076-1.",
year = "1972",
month = may,
day = "12",
doi = "10.1016/0005-2744(72)90357-9",
language = "English (US)",
volume = "268",
pages = "597--600",
journal = "BBA - Enzymology",
issn = "0005-2744",
publisher = "Elsevier BV",
number = "2",
}