Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

High activity alkaline protease was obtained when the enzyme was immobilized on Dowex MWA-1 (mesh 20-50) with 10% glutaraldehyde in chilled phosphate buffer (M/15, PH 6.5). Activity yields of the protease and rennet were 27 and 29, respectively. The highest activities appeared at 60 degrees C, pH 10 for alkaline protease and 50 degrees C, pH 4.0 for rennet. The properties of both proteases were not essentially changed by the immobilization except that the Km values of both enzymes were increased about tenfold as a result of immobilization. Both proteases in the immobilized state were more stable than those in the free state at 60 degrees C. Other peptide hydrolases, beta-galactosidase, invertase, and glucoamylase, were successfully immobilized with high activities, but lipase, hexokinase, glucose-6-phosphate dehydrogenase, and xanthine oxidase became inactive.
 ...
PMID:Preparation and properties of proteases immobilized on anion exchange resin with glutaraldehyde. 2 75

A blotting method is described to detect enzymes that do not normally yield a colored product. The method can be used for dot blotting as well as blotting after gel electrophoresis of many enzymes if the reactions they catalyze can be coupled to an oxidase or a dehydrogenase. The latter, designated "auxiliary enzymes," are preimmobilized on membranes of nitrocellulose or positively charged nylon and the reaction they catalyze is coupled with reduction of tetrazolium salt to yield colored formazan on areas of the transfer membrane occupied by the blotted enzymes. In the examples reported here, preimmobilized glucose oxidase, L-amino acid oxidase, xanthine oxidase, malate dehydrogenase, and a mixture of hexokinase and glucose-6-phosphate dehydrogenase were used as auxiliary enzymes to detect blotted invertase, leucine aminopeptidase, purine nucleoside phosphorylase, fumarase, and adenylate kinase, respectively. Detection limits varied, but never exceeded 100 ng for these enzymes. After blotting from polyacrylamide gels, the fumarase assay was the most sensitive of those investigated, detecting 10 ng of enzyme used for electrophoresis. Invertase, a glycoprotein, was detected with higher sensitivity on nitrocellulose membranes when concanavalin A was present on the membrane in addition to the auxiliary enzyme, glucose oxidase. On blots from isoelectric focusing gels, the assay detected two isozymes of purine nucleoside phosphorylase in a sample from calf spleen and at least five isozymes of this enzyme in lysates from human red cells.
 ...
PMID:Activity staining of blotted enzymes by reaction coupling with transfer membrane-immobilized auxiliary enzymes. 245 38

The toxic effect and anti-tumor activity of B-3839, a new molecular combination of pyrimidine antimetabolite 5-fluorouracil (5-FU) with the alkylating agent N-Chloroethyl-N-nitrosourea (BCNU), was compared to that of BCNU and 5-FU given alone and in physical combination. The tumor inhibitory effect of B-3839 was similar to that of BCNU given alone or combined with a low dose of 5-FU in the i.m. Walker tumor model. Furthermore, the bone marrow toxicity of BCNU was not significantly altered by either form of combination with 5-FU. The intestinal side effects, evaluated by measuring the decrease of marker enzyme (thymidine kinase, xanthine oxidase, alkaline phosphatase, sucrase, maltase) activities in isolated enterocytes, were dose-dependent and moderate. A significant, more than 30%, decrease occurred only if BCNU and 5-FU were given simultaneously or as B-3839. The molecular combination of the two drugs does not provide any additional advantage over their physical combination.
 ...
PMID:Comparison of tumor growth inhibitory and toxic effects of a new fluorouracil--nitrosourea derivative (B-3839). 297 32

We report in detail the ontogeny and the response of antioxidant enzymes to glucocorticoids in the rat small intestine. Pregnant rats in the treatment group received four injections of dexamethasone starting on days 18, 19, or 20 of gestation; fetuses were killed 2 days later. Control rats were injected with 0.9% saline solution. Postnatal rats reaching 14, 19, and 104 days of age received four injections of hydrocortisone and were killed 2 days later. Age-matched controls were injected with 0.9% saline solution. The activities of xanthine oxidase, superoxide dismutase, and catalase were measured in small intestines from fetal (20 and 21 days gestation), newborn, and older (aged 16, 21, and 106 days) rats. Xanthine oxidase rose with maturation; the major increase occurred on postnatal day 21. Catalase and superoxide dismutase rose minimally during intrauterine life. On day 16 postpartum, catalase and superoxide dismutase values were 160% and 60%, respectively, higher than at birth. Glucocorticoid administration stimulated maltase and sucrase activities, but had no effect on the antioxidant enzymes or xanthine oxidase.
 ...
PMID:Maturation of antioxidant enzymes in rat small intestine: lack of glucocorticoid stimulation. 362 18

Wistar rats were treated with alkylating sugar alcohol derivatives, dianhydrogalactitol (DAG) and diacetyldyanhydrogalactitol (Diac-DAG), respectively. The drugs were intravenously administered as a single, bolus injection. The applied doses 2.5, 5, 10, 17 mg/kg DAG and 5, 10, 20, 40 mg/kg Diac-DAG were roughly equitoxic. The effect of these cytostatic agents was studied on the different marker enzymes (thymidine kinase, xanthine oxidase, alkaline phosphatase, sucrase, maltase) of the separated mucosa cells derived from the functional and proliferating zone of the small intestine. Both DAG and Diac-DAG inhibited the enzyme activities of the proliferating and mature enterocytes in a dose dependent fashion, primarily acting on the crypt specific thymidine kinase. The time dependent sequence in the biochemical alterations correlated well with the cytomorphological changes. The drug-induced damage was most pronounced 48 hours after a single treatment. The regeneration of the intestinal mucosa began on days 3 and 4 and was completed by day 7. Diac-DAG at equimolar concentration proved to be more toxic than DAG on the intestine as judged by the significantly higher decrease of protein content and xanthine oxidase activity.
 ...
PMID:Enzymological and morphological changes in rat intestinal mucosa following treatment with alkylating sugar alcohol derivatives. 403 42

The influence of the treatment schedule of dianhydrogalactitol on its effect on the activity of mucosal enzymes in rat intestine was studied. The effect of a single high dose (10 mg/kg) was compared with that of repeated small doses (4 x 2.5 mg/kg) given at daily intervals. At 48 h after a single high dose the activities of thymidine kinase, which is a marker of dividing crypt cells, and of alkaline phosphatase, sucrase, maltase, xanthine oxidase, which are markers of mature enterocytes, were strongly depressed. Even 96 h after the treatment low enzyme activities could be observed. Repeated small doses caused milder enzyme inhibition and almost total recovery had occurred by 96 h after administration of the last dose. The results indicate that fractionation of drug administration can reduce the toxic side-effects on the intestinal mucosa and might be partly responsible for the higher therapeutic index of such schedules in experimental tumor models.
 ...
PMID:Effect of a single high dose and repeated small doses of dianhydrogalactitol (DAG; NSC-132313) on rat intestinal mucosa. 641 95

The use of printing to produce 2D arrays is well established, and should be relatively facile to adapt for the purpose of printing biomaterials; however, very few studies have been published using enzyme solutions as inks. Among the printing technologies, inkjet printing is highly suitable for printing biomaterials and specifically enzymes, as it offers many advantages. Formulation of the inkjet inks is relatively simple and can be adjusted to a variety of biomaterials, while providing nonharmful environment to the enzymes. Here we demonstrate the applicability of inkjet printing for patterning multiple enzymes in a predefined array in a very straightforward, noncontact method. Specifically, various arrays of the enzymes glucose oxidase (GOx), invertase (INV) and horseradish peroxidase (HP) were printed on aminated glass surfaces, followed by immobilization using glutardialdehyde after printing. Scanning electrochemical microscopy (SECM) was used for imaging the printed patterns and to ascertain the enzyme activity. The successful formation of 2D arrays consisting of enzymes was explored as a means of developing the first surface confined enzyme based logic gates. Principally, XOR and AND gates, each consisting of two enzymes as the Boolean operators, were assembled, and their operation was studied by SECM.
...
PMID:Multienzyme Inkjet Printed 2D Arrays. 2621 72