Esterase SeE ofStreptococcus equissp.equiis a novel nonspecific carboxylic ester hydrolase

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Esterase SeE of Streptococcus equi ssp. equi is a novel nonspecific carboxylic ester hydrolase.

Extracellular carboxylic ester hydrolases are produced by many bacterial pathogens and have been shown recently to be important for virulence of some pathogens. However, these hydrolases are poorly characterized in enzymatic activity. This study prepared and characterized the secreted ester hydrolase of Streptococcus equi ssp. equi (designated SeE for S. equi esterase). SeE hydrolyzes ethyl ace...

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Carboxylic Ester Hydrolase in Acute Pancreatitis a Clinical and Experimental Study

Diagnosis of acute pancreatitis (AP) is erroneous in up to one third of patients when based on clinical criteria and elevated serum amylase values. Furthermore, according to autopsy reports fatal pancreatitis remains clinically undiagnosed in 22 to 86 % of hospitalised patients. Consequently, search for better methods for the diagnosis of AP seems not only justified but urgent. The pancreas sec...

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Monocyte Nonspecific Esterase: Purification and Subunit Structure

Monocyte nonspecific esterase has been purified from cultured cells of the acute myeloid leukemia cell line. ML-l. The purified enzyme shows the characteristic properties of the monocyte neutral serine carboxyI esterase, with high sensitivity to organophosphorus inhibitors and sodium fluoride inhibitor. The enzyme is a membrane protein which in the native state exists as a monomer of a mol wt o...

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Monocyte nonspecific esterase: purification and subunit structure.

Monocyte nonspecific esterase has been purified from cultured cells of the acute myeloid leukemia cell line, ML-1. The purified enzyme shows the characteristic properties of the monocyte neutral serine carboxyl esterase, with high sensitivity to organophosphorus inhibitors and sodium fluoride inhibitor. The enzyme is a membrane protein which in the native state exists as a monomer of a mol wt o...

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Carboxylic ester hydrolases of rat pancreatic juice.

An attempt was made to establish the number and characteristics of the enzymes in pancreatic juice that hydrolyze nitrogen- and phosphorus-free esters of fatty acids. For this purpose model compounds were hydrolyzed by lyophilized rat pancreatic juice under conditions that accelerated or inhibited the reactions. Although it is not established with certainty, it is suggested that three enzymes a...

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ژورنال

عنوان ژورنال: FEMS Microbiology Letters

سال: 2008

ISSN: 0378-1097,1574-6968

DOI: 10.1111/j.1574-6968.2008.01377.x