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Esterase
About: Esterase is a research topic. Over the lifetime, 7622 publications have been published within this topic receiving 168270 citations.
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TL;DR: The Tween 80 assay to detect lipolytic activities in agar media was evaluated and the activity was similar to that obtained with p-nitrophenyl butyrate; the enzyme activities were between the esterase and lipase categories.
Abstract: The Tween 80 assay to detect lipolytic activities in agar media was evaluated A spectrophotometric assay for Tween 80 hydrolysis was established The specific activities with Tween 80, as well as with some conventional lipase-type and esterase-type substrates, were measured using several lipases and esterases The activity with Tween 80 was similar to that obtained with p-nitrophenyl butyrate; the enzyme activities with both substrates were between the esterase and lipase categories © Rapid Science Ltd 1998
86 citations
TL;DR: The production, purification, characterizations, enhancement of activity and stability, immobilization of the enzyme and its applications in various industries have been discussed.
86 citations
TL;DR: It has been observed that acid phosphatase activity may be similaxly localized and this is particularly noticeable with the formol-ealcium-fixed tissue, when the enzyme once again appears to be associated with intracellular particles in the vicinity of the bile canaliculi.
Abstract: I t has been shown by means of a histochemical staining technique, considered to conform to sound basic principles, that esterase activity is mainly associated with microscopic structures around the bile canaliculi of formol-calcium-fixed rat liver (1). A comparable, but less precise, localization is given by entirely independent histochemical techniques (1, 2). I t has also been observed that acid phosphatase activity may be similaxly localized (3) and this is particularly noticeable with the formol-ealcium-fixed tissue, when the enzyme once again appears to be associated with intracellular particles in the vicinity of the bile canaliculi (4). This suggests tha t the two enzymes may be associated with the same intracellular structures. However, the enzymes behave very differently in liver dispersions fractionated by differential centrifugation. Whereas the microsomes contain most of the esterase activity as tested against a variety of substrates (5-9), acid phosphatase has been found to belong to an intermediate group of cytoplasmic particles, comparable in size to the smaller mitochondria (7, 10-13). A number of other acid hydrolases appear to be associated with these particles, which have been termed lysosomes for this reason (11). Preliminary electron microscope investigations (14) have shown that they may be identical with the dense peribiliary bodies described by Rouiller (15) and by Palade and Siekevitz (16).
85 citations
TL;DR: Analysis of the activity of the acidlipase isoenzyme in cell extracts from human-Chinese hamster somatic cell hybrids demonstrated the concordant segregation of the gene locus for lysosomal acid lipase with the glutamate oxaloacetate transaminase-1 (GOT1) enzyme marker for human chromosome 10.
85 citations
TL;DR: The structure of an active site mutant in complex with the reaction product, acetate, reveals details of the putative oxyanion binding site, and suggests that substrates bind predominantly through non-specific contacts with protein hydrophobic residues.
85 citations