Results 191 to 200 of about 6,120 (217)
Some of the next articles are maybe not open access.
Anandamide Amidohydrolase from Porcine Brain
1997Ethanolamide of arachidonic acid was isolated from porcine brain as an endogenous ligand for cannabinoid receptors, and referred to as anandamide.1 In consideration of various biological activities of anandamide,2 it is very important to elucidate how the production and degradation of this new compound are regulated by enzymes within the cells.
Shozo Yamamoto +3 more
openaire +2 more sources
Distribution and characterization of anandamide amidohydrolase in mouse brain and liver
Life Sciences, 1998Anandamide (N-Arachidonoylethanolamine) amidohydrolase catalyzing hydrolysis of anandamide was characterized in mice. The enzymatic activity was highest in the liver, followed by the brain and testis. Negligible activity was found in heart, lung and spleen. The activity in brain and liver was mainly localized in the microsomal fractions.
Ikuo Yamamoto +6 more
openaire +3 more sources
Partial purification and characterization of an amidohydrolase from soybean
Phytochemistry, 1969Abstract A soluble enzyme with amidohydrolase activity was isolated from the roots of soybean seedlings and purified 45-fold by ammonium sulfate fractionation, gel filtration and cellulose ion-exchange chromatography. The enzyme hydrolyzed primarily N α -benzoyl- dl -arginine p -nitroanilide and to a slight extent the p -nitroanilides of glycine ...
G. Graf, Robert E. Hoagland
openaire +2 more sources
Effects of Acidity and Alkalinity on the Stability of Amidohydrolases in Freshwater
Journal of Environmental Quality, 1983AbstractThe influence of acidity and alkalinity on the enzymatic hydrolysis of amide‐N in the aquatic system was investigated by determining the stability of L‐asparaginase (EC [Enzyme Commission] 3.5.1.1). L‐glutaminase (EC 3.5.1.2), and amidase (EC 3.5.1.4), and urease (EC 3.5.1.5) with respect to pH in three freshwater lakes.
A. L. Page, W. T. Frankenberger
openaire +2 more sources
Identification of Caerulomycin A Gene Cluster Implicates a Tailoring Amidohydrolase
Organic Letters, 2012The biosynthetic gene cluster for caerulomycin A (1) was cloned and characterized from the marine actinomycete Actinoalloteichus cyanogriseus WH1-2216-6, which revealed an unusual hybrid polyketide synthase (PKS)/nonribosomal peptide synthetase (NRPS) system.
Weiming Zhu +8 more
openaire +3 more sources
Penicillin amidohydrolase productivity of locally isolated bacterial species
Folia Microbiologica, 1991Penicillin amidohydrolase productivity of four locally isolated bacterial species is described. Organisms were identified as Escherichia coli, Pseudomonas aeruginosa, Sarcina lutea and Bacillus megaterium. Highest enzyme productivity of 3.2 U/mL with a corresponding dry cell mass of 4.5 g/L was recorded from S. lutea.
D. Shaikh, S M S Zoha, Z. A. Mahmood
openaire +3 more sources
Stabilization of Penicillin Amidohydrolase Immobilized on Eupergit C
1982Carrier bound enzymes are playing an increasing important role in industrial production, in part through development of carriers with good filtration properties and high loading capacity. Economically it is important how often one can reuse carrier bound enzymes. Therefore, we have looked at higher stability under repeated use. Since dithiols are known
K. Sauber, D. M. Kramer
openaire +2 more sources
Penicillin acylases as amidohydrolases and acyl transfer catalysts
Biotechnology Letters, 1981The hypothesis that an acyl-enzyme intermediate of the esterases from Xanthomonas citri and Acetobacter turbidans is reponsible for the acylation of 7-aminodeacetoxycephalosporanic acid and similar compounds by esters of amino acids, recently proposed by Kato, also accounts for the kinetics of hydrolysis of penicillin G by the amidohydrolase from E ...
openaire +2 more sources

