Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The cell-associated and extracellular enzymatic activities were examined in a total of 10 Penicillium marneffei isolates. Both mycelia and yeast expressed alkaline phosphatase, acid phosphatase and naphthol-AS-BI-phosphohydrolase activities, whereas a variety of other enzyme activities, including trypsin, chymotrypsin and alpha-fucosidase were absent. There was some inter-isolate variation in both mycelia and yeast in the activities of other enzymes such as esterases and galactosidases. Enzyme activities did not change significantly over the course of culturing in three representative isolates.
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PMID:Analysis of the enzymatic activity of mycelial and yeast phases of Penicillium marneffei. 1064 27

The high molecular weight arylamidase-alkaline phosphatase-complex from rat kidney microsomes [1] was carefully dissociated by means of treatment with several hydrolytic enzymes or by acidification. Trypsin, chymotrypsin and pronase cause a selective solubilization of the enzymes discernible at their different electrophoretic mobility in polyacrylamide gel. The lower migrating zone represents phosphatase, the faster migrating zone shows arylamidase activity (molecular weights 180,000 and 172,000, respectively). Incubation of the complex with papain, lipase, neuraminidase or hyaluronidase and incubation at acid conditions (pH optimum 5.0) in the absence of any enzyme also yields in the appearance of two protein bands. In contrast to the alkaline hydrolases the acid hydrolases, the pH 5-treatment and with a certain degree also the lipase liberate a second arylamidase zone lying in the phosphatese containing zone during polyacrylamide gel electrophoresis. Treatment with SDS and subsequent SDS-polyacrylamide gel electrophoresis also results in a dissociation of the complex, but only in one protein fragement (approx, molecular weight 205,000).
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PMID:??? 1194 35

A nondiapause strain of the gypsy moth offers an additional tool for evaluating the regulation of diapause in this species. Patterns of protein expression in the gut and gut enzyme activity distinguished the two strains. Synthesis of a 55kDa gut protein, previously linked to diapause, began 14days after oviposition in both the diapause (D) and nondiapause (ND) strains. Though synthesis of this protein persisted in the D strain, its synthesis decreased after day 18 in the ND strain. In the D strain, activity of the proteolytic enzymes (trypsin, chymotrypsin, elastase, aminopeptidase) and esterase remained low, while activity of all of these enzymes increased dramatically in the ND strain 18-20days after oviposition. By contrast, alkaline phosphatase (ALP) activity was high in both strains 15-17days after oviposition, activity remained high in the D strain but in the ND strain activity then decreased. Patterns of ALP zymograms were similar in the two strains on day 15, but later a band of high mobility appeared only in the D strain. When 20-hydroxyecdysone was added to hanging drop cultures containing ND pharate larvae 15days after oviposition, the larvae assumed the characteristics of diapause larvae: the 55kDa gut protein was synthesized, the ALP zymogram revealed the characteristic diapause pattern, and they failed to ingest culture medium. The fact that 20-hydroxyecdysone could elicit these responses in ND individuals further supports previous results indicating that ecdysteroids promote the induction and maintenance of the pharate larval diapause in this species.
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PMID:Further evidence that diapause in the gypsy moth, Lymantria dispar, is regulated by ecdysteroids: a comparison of diapause and nondiapause strains. 1277 Apr 59

A study was conducted to investigate changes in the development of the gastrointestinal tract (GIT) in relation to body growth of growing ostriches. There was an 11-fold increase (P < 0.001) in body weight between 3 and 72 days of age. The relative (to body weight) weight of the proventriculus/gizzard, caeca and colon also increased (P < 0.001) with age. The relative weight of the small intestine peaked at 41 days of age and then tended to decline (P < 0.05) subsequently. The relative weight of the pancreas peaked at 27 days of age and remained fairly stable thereafter. The activities of chymotrypsin and lipase declined (P < 0.001) with age between 3 and 72 days. At 3 days of age, the protein content of the duodenal mucosal homogenate was higher (P < 0.001) than that of the jejunum or ileum, but at all subsequent periods the jejunal protein content was the highest. The protein content of the intestinal brush-border membrane was higher (P < 0.001) at the jejunum than at the duodenum or ileum. The specific activity of maltase declined (P < 0.001) with age in all three regions, most especially between 3 and 27 days of age. The activity of alkaline phosphatase (AP) at 41 and 55 days of age was higher (P < 0.001) in the duodenum than in the jejunum or ileum. The activity of AP fluctuated with age in the duodenum but there was a more defined decline (P < 0.001) with age in the jejunum and ileum. The relative protein content of the liver increased (P < 0.001) with age, with two peaks at 27 and 55 days of age. Arginase activity was not detected in the liver of 3-day old chicks and was not significantly affected by age between 27 and 72 days of age. The pattern of development observed is similar to that in growing poultry. There is, however, a need for evaluation at closer intervals in early life as well as an in-depth assessment of the morphometry of the intestinal mucosa.
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PMID:Development of the digestive tract in the ostrich (Struthio camelus). 1290 66

Although the structure of an enzyme is often depicted as static, it is dynamic. Hence, a population of chemically identical enzymes has not one, but a distribution of structures at any moment in time. Does this have an effect on the activity of the enzyme? This article reviews experiments designed to test the hypothesis that this distribution of structures results in a distribution of enzyme activities. The experiments reviewed here use different enzymes, falvin adenine dinucleotide, beta-galactosidase, alkaline phosphatase, exonuclease I, lactate dehydrogenase I, alpha-chymotrypsin, the 20S proteasome, and horseradish peroxidase. All experiments come to the same conclusion, when measured individually, apparently identical enzymes show a distribution in rates of activity.
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PMID:Diversity in the activity of individual enzymes. 1637 26

We have studied the immunochemical and biochemical differences in 12 Aspergillus fumigatus strains isolated from different sources. The enzymatic activity of all these strains were studied by a rapid enzyme detection method (API-ZYM). One of 12 strains studied produced alkaline phosphatase, while two produced chymotrypsin, and three produced trypsin. By SDS-PAGE we studied proteins present in the antigen extracts from all 12 strains. Several of the protein bands were unique and may be used to differentiate the strains. One such protein is the 58 kDa band present in the mycelial extract and the 33 kDa in the culture filtrate. By crossed immunoelectrophoresis, differentiation of the strains isolated from cystic fibrosis patients can be made based on a few specific precipitin arcs developed against anti-Aspergillus rabbit serum.
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PMID:Immunochemical reactivity of Aspergillus fumigatus antigens from different sources. 1685 71

A rapid, homogenous, antibody-free assay for phosphatase enzymes was developed using the phosphorescent platinum (II)-coproporphyrin label (PtCP) and time-resolved fluorescent detection. An internally quenched decameric peptide substrate containing a phospho-tyrosine residue, labeled with PtCP-maleimide and dabcyl-NHS at its termini was designed. Phosphatase catalysed dephosphorylation of the substrate resulted in a minor increase in PtCP signal, while subsequent cleavage by chymotrypsin at the dephosphorylated Tyr-Leu site provided a 3.5 fold enhancement of PtCP phosphorescence. This phosphorescence phosphatase enhancement assay was optimized to a 96 well plate format with detection on a commercial TR-F plate reader, and applied to measure the activity and inhibition of alkaline phosphatase, recombinant human CD45, and tyrosine phosphatases in Jurkat cell lysates within 40 min. Parameters of these enzymatic reactions such as Km's, limits of detection (L.O.D's) and IC50 values for the non-specific inhibitor sodium orthovanadate were also determined.
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PMID:Homogeneous time-resolved fluorescence assays for the detection of activity and inhibition of phosphatase enzymes employing phosphorescently labeled peptide substrates. 1738 66

1. A total of 320 1-d-old Arbor Acres broiler chicks were used to investigate the effect of Cu(2+)-loaded montmorillonite (CM) on the growth performance, intestinal morphology and activities of brush border enzyme in the intestinal mucosa and digestive enzyme in the intestinal digesta of broilers. 2. The chicks were assigned randomly into 4 groups with 80 chicks per treatment. The 4 dietary treatments were: basal diet only (control group), basal diet + 2 g montmorillonite/kg, basal diet + 1 g CM/kg, and basal diet + 2 g CM/kg. The chicks were raised in cages and feed and water were provided ad libitum for a period of 42 d. 3. The addition of CM to the diet of broilers significantly increased body weight and feed efficiency. Similarly, birds receiving montmorillonite had higher feed efficiency than the control after 42 d of feeding. 4. Data on villus height and crypt depth for duodenum, jejunum and ileum indicated that treating the diet of broilers with either CM or montmorillonite improved the mucosal morphology of the small intestine. 5. The presence of CM in the diet of broilers significantly increased the activities of maltase, aminopeptidase N and alkaline phosphatase in small intestinal mucosa. However, the activities of protease, trypsin, chymotrypsin, amylase and lipase in small intestinal digesta of broilers fed on the CM-supplemented diet were slightly higher than control values.
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PMID:Intestinal morphology, brush border and digesta enzyme activities of broilers fed on a diet containing Cu2+-loaded montmorillonite. 1821 Feb 91

Reactive polymers have been prepared by copolymeriz-ing N-isopropyl acrylamide (NIPAM) with N-acryloxy-succinimide (NASI) or glycidyl methacrylate (GMA). The amino groups of ligands could react with the residues of NASI or GMA and the polymers could be precipitated by temperature and/or salinity variation, since they contained the NIPAM residues. As a model, p-aminobenza-midine, a trypsin inhibitor, was attached to the polymers to form water-soluble macroligands, capable of selectively binding trypsin from a trypsin-chymotrypsin solution. After precipitation of the macroligand-trypsin complex, followed by dissociation, approximately 82% trypsin was isolated. The NIPAM-GMA copolymer was also reacted with immunogammaglobulin (IgG) and alkaline phosphatase (AP). It was demonstrated that the IgG bearing polymer was able to bind protein A and the whole complex was precipitable. The reactive polymer was also used for direct immobilization of AP which was active in repeated reactions.
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PMID:Syntheses and applications of water-soluble reactive polymers for purification and immobilization of biomolecules. 1858 16

The Fmoc-protected heptasaccharide asparagine building block beta-GlcNAc-(1-->2)-alpha-Man-(1-->3)-[beta-GlcNAc-(1-->2)-alpha-Man-(1-->6)]beta-Man-(1-->4)-beta-GlcNAc-(1-->4)-beta-GlcNAc-(Fmoc)Asn was obtained by chemical synthesis. Two flexible strategies were developed with optimized conditions for the simultaneous debenzylation of the sugar and the amino acid part. The heptasaccharide asparagine building block is a partial structure of many glycoproteins and can be used for glycopeptide synthesis in solution and on the solid phase. In this work the heptasaccharide asparagine was elongated in solution to an Fmoc-glycopentapeptide methylester. After chemical cleavage of the Fmoc group the methylester was removed enzymatically by chymotrypsin. The use of beta-(1-->4)-galactosyltransferase and alpha-(2-->6)-sialyltransferase in the presence of alkaline phosphatase allowed the efficient transfer of four sugar units to the acceptor resulting in an undecasaccharide glycopentapeptide.
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PMID:Synthesis of an Fmoc-Asn-heptasaccharide building block and its application to chemoenzymatic glycopeptide synthesis. 2041 27


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