Acid lipase activity of human lymphocytes. Biochim Biophys Acta 1979 Feb 26;572(2):225-34
Date
02/26/1979Pubmed ID
427176DOI
10.1016/0005-2760(79)90038-9Scopus ID
2-s2.0-0018741951 (requires institutional sign-in at Scopus site) 31 CitationsAbstract
Acid lipase activity was examined in human leukocytes using 4-methylumbelliferyl esters in a fluorimetric assay. Mononuclear leukocytes had 10--15 times the acid lipase activity of polymorphonuclear leukocytes. The enzyme activity was highest using the oleate ester of 4-methylumbelliferone at pH 4.0, in the presence of L-alpha-phosphatidylcholine and taurodeoxycholic acid (sodium salt). Acid lipase activity was inhibited by diethylaminoethoxyhexestrol, sodium chloride and fluoride, potassium chloride, calcium chloride and albumin, but was unaffected by diethyl p-nitrophenyl phosphate or sulphydryl reagents. There were at least two forms of acid lipase activity: one (A form) was sensitive to heart inactivation (56 degrees C) and corresponded to the enzyme deficient in patients with Wolman's disease; the other (B form) was resistant to heat inactivation and corresponded to the residual enzyme activity found in Wolman's disease.
Author List
Coates PM, Cortner JA, Hoffman GM, Brown SAAuthor
George M. Hoffman MD Chief, Professor in the Anesthesiology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Bile Acids and SaltsHumans
Kinetics
Lipase
Lymphocytes
Monocytes
Neutrophils
Phosphatidylcholines
Substrate Specificity
