Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The larval serum protein-2 gene (Lsp-2) of Drosophila melanogaster is expressed at a very high level in the fat body of third-instar larvae. Here we report that Lsp-2 transcription in adult flies produces a unique mRNA localized in the adult adipose tissue of the head in both sexes. To identify regulatory regions of this Drosophila gene, Lsp-2 5'-flanking DNA sequences were fused to the E. coli beta-galactosidase gene (lacZ). Transient expression of the hybrid gene in third-instar larvae indicates that 230 bp just upstream from the 'TATA box' of the Lsp-2 gene are sufficient for larval fat body-specific expression.
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PMID:Fat-body-specific expression of the Drosophila Lsp-2 gene. 136 81

Mice immunized with the recombinant antigen 11.1 beta-galactosidase, consisting of 22 repeats of the nine-amino acid unit from Plasmodium falciparum antigen 11.1, produced antibodies reacting with human serum albumin. A positive reaction was observed in dot-blot assays, in enzyme-linked immunosorbent assay and on immunoblots of sodium dodecyl sulfate polyacrylamide gels as well as two-dimensional gels. Binding was specific for human albumin, as no reaction could be detected on bovine serum albumin, hen egg ovalbumin, rat serum albumin or another abundant human serum protein, the alpha 2-macroglobulin. In addition, rabbit antibodies raised to human serum albumin reacted with keyhole lympet hemocyanin coupled to synthetic dimers of the nine-amino acid repeats of the P. falciparum 11.1 antigen. These data indicate antigenic relationship between the 11.1 antigen and human albumin. The proteins have a short sequence of homology in a region where human serum albumin differs from the albumins of other species.
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PMID:Cross-reaction of antibodies to the nine-amino acid repeats of Plasmodium falciparum antigen 11.1 with human serum albumin. 153 76

The expression vector lambda gt11Amp3 has been used to construct a cDNA library from rat liver polyadenylated RNA. Clones expressing antigenic determinants for rat albumin, transferrin, transthyretin, apolipoprotein E and apolipoprotein AII have been identified. Albumin clones containing cDNA inserts ranging from 0.9 kb to 1.9 kb were further identified by restriction mapping and nucleic acid sequencing. The largest insert contained the entire coding sequence for albumin. Characterization of the expressed proteins by acrylamide gel electrophoresis followed by immunological detection indicated that the proteins were produced as hybrids linked to the bacterial beta-galactosidase. A cDNA library for human liver polyadenylated RNA has also been constructed. Clones expressing antigenic determinants for human serum albumin, transferrin and apolipoproteins AI, AII, AIV and E have been isolated and their identity established by nucleotide sequencing and restriction mapping. Both rat and human serum protein cDNA clones are currently being used to study the tissue specific expression of serum proteins and for the isolation and characterization of the corresponding genes.
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PMID:Isolation and characterization of genes for blood proteins. 330 67

The Larval serum protein-2 gene (Lsp-2) of Drosophila melanogaster is uniquely expressed in the fat body tissue from the beginning of the third instar to the end of adult life. Accumulation of the larval Lsp-2 transcript is enhanced by 20-hydroxyecdysone. To study the molecular basis for ecdysone regulated Lsp-2 activity, deletion mutants of the Lsp-2 5'-flanking region were constructed by fusion to either the Escherichia coli chloramphenicol acetyltransferase (CAT) gene or to an hsp70-lacZ hybrid gene encoding beta-galactosidase. Constructs transfected into Drosophila S2/M3 cells were shown to confer transient ecdysone inducibility on the reporter genes. A single functional ecdysone response element (EcRE) was localized at position -75 relative to the Lsp-2 transcription initiation site. In gel mobility shift assays using fat body nuclear extracts or nuclear receptors synthesized in vitro, a 27-bp sequence harboring the EcRE bound both the Drosophila ecdysone receptor and the Drosophila retinoid-X homologue, Ultraspiracle, in a cooperative manner. Competition experiments indicate that the affinity of the Lsp-2 EcRE for the ecdysone receptor complex is comparable to that of the canonical EcRE of the hsp27 gene and is at least 4-fold greater than that of Fbp1, another fat body-specific Drosophila gene. Our results suggest that structural features of this EcRE determine its ability to induce ecdysone responsiveness at a lower ligand concentration and may form the basis for differential hormone responsiveness within the fat body.
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PMID:Characterization of an EcR/USP heterodimer target site that mediates ecdysone responsiveness of the Drosophila Lsp-2 gene. 854 20

This immunological study involved individual injection of the three Schistosoma mansoni antigens (Ags). soluble egg antigen (SEA), cercarial antigen preparation (CAP) or soluble worm antigen preparation (SWAP) in three rabbits groups (Ag). respectively. Three other groups each received the same specific antigen conjoined with administration of L-carnosine (Ag-C). Determination of three hepatic parameters and ten serum proteins was done. These were total protein, glycogen content and glycogen phosphorylase b activity of liver as well as serum total protein and nine protein fractions [alpha2-macrglobulin; beta-galactosidase; phosphorylase b; serum albumin; fumarase; carbonic anhydrase; beta-lactoglobulin; alpha-lactalbumin and aprotinin]. Conjoined carnosine treatment produced numerous variations. SEA-I-C group presented sex decreased parameters. In CAP-I-C animals hepatic glycogen content was increased while phosphorrylase b activity was decreased as well as seven the concentration of serum parameters; total serum protein, alpha2-macroglobulin, phosphorylase b, albumin, fumarase, carbonic anhydrase, alpha-lactalbumin and aprotinin. In SWAP-I-C group the concentration of only one fraction was decreased; carbonic anhydrase. In batch A both the Ags. of the egg and cercaria, developmental stages having transient residence in the animal host, showed more affection by the specific Ag. Although, carnosine modified the results of all the three groups in batch B yet, its effect on both the egg and cercaria Ags. was still more than that of worm.
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PMID:Biochemical modifications induced in rabbits by Schistosoma mansoni antigens and the beneficial effect of carnosine treatment. 1588 Oct 9

Bioluminescence using the reporter enzyme firefly luciferase (Fluc) and the substrate luciferin enables non-invasive optical imaging of living animals with extremely high sensitivity. This type of analysis enables studies of gene expression, tumor growth, and cell migration over time in live animals that were previously not possible. However, a major limitation of this system is that Fluc activity is restricted to the intracellular environment, which precludes important applications of in vivo imaging such as antibody labeling, or serum protein monitoring. In order to expand the application of bioluminescence imaging to other enzymes, we characterized a sequential reporter-enzyme luminescence (SRL) technology for the in vivo detection of beta-galactosidase (beta-gal) activity. The substrate is a "caged" D-luciferin conjugate that must first be cleaved by beta-gal before it can be catalyzed by Fluc in the final, light-emitting step. Hence, luminescence is dependent on and correlates with beta-gal activity. A variety of experiments were performed in order to validate the system and explore potential new applications. We were able to visualize non-invasively over time constitutive beta-gal activity in engineered cells, as well as inducible tissue-specific beta-gal expression in transgenic mice. Since beta-gal, unlike Fluc, retains full activity outside of cells, we were able to show that antibodies conjugated to the recombinant beta-gal enzyme could be used to detect and localize endogenous cells and extracellular antigens in vivo. In addition, we developed a low-affinity beta-gal complementation system that enables inducible, reversible protein interactions to be monitored in real time in vivo, for example, sequential responses to agonists and antagonists of G-protein-coupled receptors (GPCRs). Thus, using SRL, the exquisite luminescent properties of Fluc can be combined with the advantages of another enzyme. Other substrates have been described that extend the scope to endogenous enzymes, such as cytochromes or caspases, potentially enabling additional unprecedented applications.
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PMID:Imaging beta-galactosidase activity in vivo using sequential reporter-enzyme luminescence. 1968 14