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Side 1 fra 78 resultater
Purification and Characterization of Two Benzoyl-l-Tyrosine p-Nitroanilide Hydrolases from Etiolated Leaves of Zea mays L.
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Two benzoyl-l-tyrosine p-nitroanilide hydrolases (BTPAases I and II) were purified from the etiolated leaves of Zea mays L. and characterized. BTPAase I was electrophoretically homogeneous and consisted of two identical subunits having a molecular weight of 53,000. The molecular weight of BTPAase II
Purification and characterization of benzoyl-L-arginine p-nitroanilide hydrolase from etiolated leaves of Zea mays.
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Benzoyl-L-arginine p-nitroanilide hydrolase in the etiolated leaves of Zea mays L. has been purified 1,266-fold by a combination of gel filtration, ion exchange, and hydrophobic chromatography with a recovery of 13%. The specific activity of the purified enzyme is 5.7 units/mg protein. The enzyme is
Jejunal brush border hydrolase activity is higher in tallow-fed pigs than in corn oil-fed pigs.
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We tested the effect of dietary fat on the lipid composition and hydrolase activity of jejunal brush border membranes in piglets. Eighteen 5-wk-old piglets were divided into three groups and for 4 wk fed either an unsaturated low fat diet (3.2% corn oil), an unsaturated high fat diet (17.2% corn
Global and grain-specific accumulation of glycoside hydrolase family 10 xylanases in transgenic maize (Zea mays).
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In planta expression of cell wall degrading enzymes is a promising approach for developing optimized biomass feedstocks that enable low-cost cellulosic biofuels production. Transgenic plants could serve as either an enzyme source for the hydrolysis of pretreated biomass or as the primary biomass
Crystallographic structure of ChitA, a glycoside hydrolase family 19, plant class IV chitinase from Zea mays.
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Maize ChitA chitinase is composed of a small, hevein-like domain attached to a carboxy-terminal chitinase domain. During fungal ear rot, the hevein-like domain is cleaved by secreted fungal proteases to produce truncated forms of ChitA. Here, we report a structural and biochemical characterization
Differential expression of peroxiredoxin 6, annexin A5 and ubiquitin carboxyl-terminal hydrolase isozyme L1 in testis of rat fetuses after maternal exposure to di-n-butyl phthalate.
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OBJECTIVE
To isolate and identify differentially expressed proteins in testis of rat fetuses after maternal exposure to di-n-butyl phthalate (DBP).
METHODS
Pregnant rats were daily treated by gavage with 1 ml/kg corn oil or 750 mg/kg DBP from GD14 to GD18. We used the technique of proteomic analysis
Recognition of corn defense chitinases by fungal polyglycine hydrolases.
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Polyglycine hydrolases (PGH)s are secreted fungal endoproteases that cleave peptide bonds in the polyglycine interdomain linker of ChitA chitinase, an antifungal protein from domesticated corn (Zea mays ssp. mays). These target-specific endoproteases are unusual because they do not cut a specific
The lysosome-concept in plants : II. Location of acid hydrolases in maize root tips.
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The sedimentability of eight acid hydrolases in an homogenate from root tips of Zea mays (L.) varied between 13% (α-glucosidase) and 46% (β-N-acetylglucosaminidase) of the total activity. Between 20% and 30% of total activity of the majority of acid hydrolases examined was sedimentable.High specific
A Pseudomonas aeruginosa PAO1 acetylcholinesterase is encoded by the PA4921 gene and belongs to the SGNH hydrolase family.
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Through the use of molecular and biochemical experiments and bioinformatic tools, this work demonstrates that the PA4921 gene of the Pseudomonas aeruginosa PAO1 genome is a gene responsible for cholinesterase (ChoE) activity. Similar to the acetylcholinesterase (AchE) of Zea mays, this ChoE belongs
Computational analysis of glycoside hydrolase family 1 specificities.
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Glycoside hydrolase family 1 consists of beta-glucosidases, beta-galactosidases, 6-phospho-beta-galactosidases, myrosinases, and other enzymes having similar primary and tertiary structures but diverse specificities. Among these enzymes, beta-glucosidases hydrolyze cellobiose to glucose, and
A specific enzyme hydrolyzing 6-O(4-O)-indole-3-ylacetyl-beta-D-glucose in immature kernels of Zea mays.
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The purification of 6-O(4-O)-indole-3-ylacetyl-beta-D-glucose (IAGlc) hydrolase from immature kernels of maize (Zea mays) was undertaken to separate this enzyme from 1-O-IAGlc hydrolase and beta-glucosidase. Partially purified 6-O(4-O)-IAGlc hydrolase was found to be the specific enzyme catalyzing
The role of gibberellic acid in the hydrolysis of endosperm reserves in Zea mays.
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Excised maize (Zea mays L.) endosperms incubated in buffer rapidly degrade their starch and protein reserves. These processes are not markedly stimulated by addition of gibberellic acid (GA3). However protease and α-amylase production are strongly inhibited by abscisic acid, and this inhibition can
Faecal hydrolase activity as determined by radial enzyme diffusion: a new method for detecting pancreatic dysfunction in the dog.
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A simple method was developed of measuring pancreatic hydrolase activities by allowing canine faecal, intestinal or pancreatic samples to diffuse in agar gels containing a substrate (Ca-paracaseinate, starch, corn oil). In faecal samples the protease determination proved most valuable. However, a
Cholesteryl ester hydrolase activity in adrenal homogenates from normal and essential fatty acid-deficient female rats.
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Cholesteryl ester hydrolase was assayed in adrenal homogenates from mature female rats fed a control (corn oil-containing) or essential fatty acid (EFA)-deficient diet. Cholesteryl ester of 16:0, 18:0, 18:1, 18:2(n-6), 20:4(n-6) and 22:4(n-6) were used as substrates. In control rats, the unsaturated
Structure and function of nucleoside hydrolases from Physcomitrella patens and maize catalyzing the hydrolysis of purine, pyrimidine, and cytokinin ribosides.
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We present a comprehensive characterization of the nucleoside N-ribohydrolase (NRH) family in two model plants, Physcomitrella patens (PpNRH) and maize (Zea mays; ZmNRH), using in vitro and in planta approaches. We identified two NRH subclasses in the plant kingdom; one preferentially targets the
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