Peptide Hydrolases
Mostrando 1-12 de 47 artigos, teses e dissertações.
-
1. Cloning of a novel xylanase gene from a newly isolated Fusarium sp. Q7-31 and its expression in Escherichia coli
A strain of Q7-31 was isolated from Qinghai-Tibet Plateau and was identified as Fusarium sp. based on its morphological characteristics and ITS rDNA gene sequence analysis. It has the highest capacity of degrading cell wall activity compared with other 11 strains. To do research on its xylanase activity of Fusarium sp. Q7-31 while the degrading the rice cell
Brazilian Journal of Microbiology. Publicado em: 2012-03
-
2. Biophysical and structural studies on aspartic proteases from pathogenic parasites. / Estudos biofísicos e estruturais de aspartil proteases de parasitas patogênicos.
The purpose of this study is to compare the structure of aspartic proteases of Plasmodium falciparum and Schistosoma mansoni in different chemical environments in order to provide relevant information for future rational design of new drugs and new knowledge about the folding and dynamism of structural proteins. For this, changes in secondary and tertiary st
Publicado em: 2008
-
3. Purificação, caracterização, clonagem e seqüenciamento de β-glicosidades de Tenebrio molitor (Coleoptera) / Purification, characterization, cloning and sequencing of β-glycosidases from Tenebrio molitor (Coleoptera)
In the midgut lumen of Tenebrio molitor larvae there are 4 β-glycosidases (named 1, 2, 3a and 3b), not present in the animal food. They were purified with electrophoresis, ion exchange and hydrophobic chromatographies. β-glycosidase 1 (relative molecular weight - Mr 59,000) is unstable at 30°C but is stabilized by substrates. The enzyme hydrolyses
Publicado em: 2001
-
4. Peptide hydrolases in the brush border and soluble fractions of small intestinal mucosa of rat and man
Peptide hydrolases, catalyzing the hydrolysis of 13 dipeptides and 5 tripeptides into their respective amino acids, were studied in small intestinal mucosa and other tissues, in man and in the rat.
-
5. Intracellular Localization of Peptide Hydrolases in Wheat (Triticum aestivum L.) Leaves 1
Protoplasts from 8- to 9-day-old wheat (Triticum aestivum L.) leaves were used to isolate organelles which were examined for their contents of peptide hydrolase enzymes and, in the case of vacuoles, other acid hydrolases. High yields of intact chloroplasts were obtained using both equilibrium density gradient centrifugation and velocity sedimentation centrif
-
6. Partial Purification and Characterization of Two Peptide Hydrolases from Pea Seeds
Two peptide hydrolases have been found in pea seeds (Pisum sativum var. Greenfeast) and extensively purified by ion exchange chromatography using benzoyl-dl-arginine-p-nitroanilide as substrate. The enzymes which both have molecular weights of 65,000 can be separated by anion exchange chromatography but are otherwise virtually identical in the properties tes
-
7. The Responses of Rat Intestinal Brush Border and Cytosol Peptide Hydrolase Activities to Variation in Dietary Protein Content DIETARY REGULATION OF INTESTINAL PEPTIDE HYDROLASES
The effects of variation in dietary protein content on small intestinal brush border and cytosol peptide hydrolase activities have been investigated. One group of rats was fed a high protein diet (55% casein) and another group was fed a low protein diet (10% casein). After 1 wk, brush border peptide hydrolase activity (L-leucyl-β-naphthylamide as substrate)
-
8. Aminopeptidase C of Aspergillus niger Is a Novel Phenylalanine Aminopeptidase
A novel enzyme with a specific phenylalanine aminopeptidase activity (ApsC) from Aspergillus niger (CBS 120.49) has been characterized. The derived amino acid sequence is not similar to any previously characterized aminopeptidase sequence but does share similarity with some mammalian acyl-peptide hydrolase sequences. ApsC was found to be most active towards
American Society for Microbiology.
-
9. Two Cellobiohydrolase-Encoding Genes from Aspergillus niger Require d-Xylose and the Xylanolytic Transcriptional Activator XlnR for Their Expression
Two cellobiohydrolase-encoding genes, cbhA and cbhB, have been isolated from the filamentous fungus Aspergillus niger. The deduced amino acid sequence shows that CbhB has a modular structure consisting of a fungus-type cellulose-binding domain (CBD) and a catalytic domain separated by a Pro/Ser/Thr-rich linker peptide. CbhA consists only of a catalytic domai
American Society for Microbiology.
-
10. Molecular characterization of the extracellular poly(3-hydroxyoctanoic acid) [P(3HO)] depolymerase gene of Pseudomonas fluorescens GK13 and of its gene product.
phaZPfi, the gene encoding the extracellular poly(3-hydroxyoctanoic acid) depolymerase of Pseudomonas fluorescens GK13, was cloned, sequenced, and characterized. It comprises 837 bp and is transcribed as a monocistronic message of about 950 bp from a putative sigma 70-like promoter 32 bp upstream of the ATG start codon. The deduced protein of 278 amino acids
-
11. A covalent linkage between daunorubicin and proteins that is stable in serum and reversible by lysosomal hydrolases, as required for a lysosomotropic drug-carrier conjugate: in vitro and in vivo studies.
Daunorubicin (DNR) has been conjugated to succinylated serum albumin by an amide bond joining the amino group of the drug and a carboxyl side chain of the protein either directly or with the intercalation of a peptide spacer arm varying from one to four amino acids. During in vitro incubation with lysosomal hydrolases, intact DNR could be released extensivel
-
12. Characterization of an Acetyl Xylan Esterase from the Anaerobic Fungus Orpinomyces sp. Strain PC-2
A 1,067-bp cDNA, designated axeA, coding for an acetyl xylan esterase (AxeA) was cloned from the anaerobic rumen fungus Orpinomyces sp. strain PC-2. The gene had an open reading frame of 939 bp encoding a polypeptide of 313 amino acid residues with a calculated mass of 34,845 Da. An active esterase using the original start codon of the cDNA was synthesized i
American Society for Microbiology.