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

A bioautographic assay was developed for the visualization of aminoacylase-1 (N-acylamino acid aminohydrolase, ACY-1; EC 3.5.1.14) after zone electrophoresis. Bioautography and species differences in electrophoretic mobility of ACY-1 made it possible to investigate the chromosome assignment of the gene for human ACY-1 using human--mouse somatic cell hybrids. Human ACY-1 segregated concordantly with beta-galactosidase-A (beta GALA; EC 3.2.1.23) but showed discordant segregation with 32 other markers representing 23 linkage groups. The beta GALA gene has been previously assigned to chromosome 3. From this evidence and confirming chromosome analyses, ACY-1 has been assigned to chromosome 3. A genetic polymorphism in the electrophoretic mobility of ACY was observed in mouse strains, demonstrating that this enzyme can be mapped in genetic crosses of Mus musculus.
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PMID:Bioautographic visualization of aminoacylase-1: assignment of the structural gene ACY-1 to chromosome 3 in man. 37 41

Conserved linkage groups have been found on the X and autosomal chromosomes in several mammalian species. The identification of conserved chromosomal regions has potential for predicting gene location in mammals, particularly in humans. The genes for human aminoacylase-1 (ACY1, N-acylamino acid aminohydrolase, E.C.3.5.1.14), an enzyme in amino acid metabolism, and beta-galactosidase-A (GLB1, E.C.3.2.1.23), deficient in GM1-gangliosidosis, have been assigned to human chromosome 3. Using human-mouse somatic cell hybrids segregating translocations of human chromosome 3, expression of both ACY1 and GLB1 correlated with the presence of the p21 leads to q21 region of chromosome 3. In a previous study, assignment of these genes to mouse chromosome 9 used mouse-Chinese hamster somatic cell hybrids, eliminating mouse chromosomes. To approximate the size of the conserved region in the mouse, experiments were performed with recombinant inbred mouse strains. An electrophoretic variant of ACY-1 in mouse strains was used to map the Acy-1 gene 10.7 map U from the beta-galactosidase locus. These data suggest that there is a region of homology within the p21 leads to q21 region of human chromosome 3 and a segment of mouse chromosome 9. Since the mouse transferrin gene (Trf) is closely linked to the aminoacylase and beta-galactosidase loci, we predict that the human transferrin (TF) gene is on chromosome 3.
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PMID:Mapping of aminoacylase-1 and beta-galactosidase-A to homologous regions of human chromosome 3 and mouse chromosome 9 suggests location of additional genes. 680 86

Strains of a new type of slowly growing mycobacterium were repeatedly isolated from sputum from a patient with pulmonary disease. This photochromogenic organism grew at 22, 31, 37, and 41 degrees C, possessed catalase, acid phosphatase, esterase, beta-galactosidase, and arylsulfatase activities, and hydrolyzed Tween. It did not produce nicotinic acid or have nitrate reductase, acetamidase, benzamidase, isonicotinamidase, nicotinamidase, pyrazinamidase, succinidamidase, and acid phosphatase activities. Urease activity was variable. The organism is susceptible to ethambutol and resistant to isoniazid and streptomycin. A mycolic acid analysis revealed the presence of alpha-mycolates, alpha'-mycolates, and keto-mycolates. The results of comparative 16S rRNA sequencing placed this organism at an intermediate position between the rapidly and slowly growing mycobacteria. On the basis of the pattern of enzymatic activities and metabolic properties, the results of fatty acid analyses, and the unique 16S rRNA sequence, we propose that this organism represents a new species, for which we propose the name Mycobacterium intermedium. The type strain is strain 1669/91; a culture of this strain has been deposited in the Deutsche Sammlung von Mikroorganismen und Zellkulturen as strain DSM 44049.
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PMID:Mycobacterium intermedium sp. nov. 849 35

Multifunctional supports containing epoxy groups are here proposed as a second generation of activated supports for covalent immobilization of enzymes following the epoxy chemistry on any type of support (hydrophobic or hydrophilic ones) under very mild experimental conditions (e.g., low ionic strength, neutral pH values, and low temperatures). These multifunctional supports have been easily prepared by modifying a small fraction (10-20%) of the epoxy groups contained in commercial epoxy supports. In this way, additional groups that were able to physically adsorb proteins (e.g., cationic or anionic groups, metal chelate, phenyl boronate) are generated on the support surface. The covalent immobilization of proteins on these supports proceeds via their initial physical adsorption on the supports (via different structural features). Then, "intramolecular" covalent linkages between some nucleophilic groups of the adsorbed enzyme (e.g., amino, thiol, or hydroxy groups) and the dense layer of nearby epoxy groups on the support are established. This two-step covalent immobilization dramatically improves the very low reactivity of epoxy groups toward nonadsorbed proteins. In this way, all other relevant practical advantages of epoxy groups for protein immobilization (their high stability and their ability to form very strong linkages with several nucleophilic enzyme residues with minimal chemical modification) can be an object of universal exploitation. The use of these new multifunctional supports exhibits important advantages regarding immobilization of enzymes previously adsorbed on hydrophobic homofunctional epoxy supports: (i) hydrophilic supports can also be used for immobilization of industrial enzymes; (ii) immobilization can also be carried out at low ionic strength; (iii) every protein contained in crude extracts from Escherichia coli and Acetobacter turbidans can be immobilized by sequentially using a set of different supports; (iv) in most cases, each enzyme has been immobilized on different supports, orientated through different structural features and very likely involving different areas of its surface. For example, three industrial enzymes (penicillin G acylase, lipase, and beta-galactosidase) could be immobilized through different strategies yielding immobilized derivatives with very different activities. The best derivatives preserved 75-100% of activity corresponding to the soluble enzymes used for immobilization, while in some cases a particular immobilization protocol promoted the full inactivation of the enzyme.
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PMID:Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage. 1171 Feb 5

Glutaryl-7-amino cephalosporanic acid (GL-7ACA) acylase catalyzes the conversion of GL-7ACA to 7-amino cephalosporanic acid (7-ACA). The product 7-ACA is a starting compound for semi-synthetic cephalosporin antibiotics in industry. In order to detect the expression and specific activity of protein-engineered GL-7ACA acylase accurately, two useful detective systems for its expression has been established, in which reporter genes xylE and lacZ were fused to the downstream the GL-7ACA acylase gene acy respectively and the activity of catechol dioxygenase or beta-galactosidase could indicate the amount of acy expression.
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PMID:[Establishment of detective systems for GL-7ACA acylase expression]. 1191 Jul 63

In this manuscript, we present a new bifunctional support containing epoxide and thiol-reactive groups for its use in protein immobilization. In a first step, the proteins are reversibly immobilized by reaction of its thiol groups with the thiol-reactive groups of the support under mild experimental conditions (pH 7.0, 24 degrees C). Then, the remaining epoxides of the support can form irreversible bonds with nucleophile surface groups of the already immobilized protein in a rapid way. The partial derivatization of EP-Sepabeads (a commercial matrix containing 120 micromol epoxy groups/g drained support) was optimized, using dithiotreitol (DTT) as thiolating agent. It was possible to achieve a partial thiolation of the support proportional to the concentration of DTT used (3, 8, and 15 micromol SH groups/g wet support). The remaining epoxide content after the thiolation treatment was high (e.g., nearly 70% for the highest thiolation degree). High immobilization yields were obtained for the three model enzymes selected (60% for Penicillin G acylase, 65% and 100% for K. lactis and E. coli beta-galactosidase, respectively). In all cases, no significant immobilization onto an unmodified epoxy support was found, thus demonstrating that the first step of attachment takes place through thiol-disulfide exchange reactions. In the case of the bifunctional support, progressive formation of enzyme-support attachments involving the epoxy groups was showed by the irreversible covalent attachment of the proteins on the support. The promotion of this multipoint covalent immobilization required long incubation periods at basic pH values.
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PMID:Novel bifunctional epoxy/thiol-reactive support to immobilize thiol containing proteins by the epoxy chemistry. 1460 72