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)

NADPH-cytochrome P-450 reductase was purified from hepatic microsomes of phenobarbital and hydrocortisone-treated rats by detergent solubilization and column chromatography. This membrane protein contains 31 mol per cent hydrophobic amino acid residues, 6 half-cystine residues, and a single tryptophan residue as determined by amino acid analysis after mineral or organic acid hydrolysis. The free mobility of cytochrome P-450 reductase in sodium dodecyl sulfate was identical to that of several soluble proteins used as standards (i.e. ovalbumin, bovin serum albumin, erythrocuprein, beta-galactosidase). Molecular weight estimates from sedimentation equilibrium studies in the presence of guanidine hydrochloride (76,500) are consistent with those determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate at various per cent gel concentrations (79,000 to 80,000). Computer analysis of circular dichroism spectra of cytochrome P-450 reductase in the far ultraviolet region indicated the presence of 34 per cent alpha helical and 16 per cent beta structure. The amount of random structure was calculated to be 50 per cent.
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PMID:NADPH-cytochrome P-450 reductase. Circular dichroism and physical studies. 1 69

beta-Galactosidase (EC 3.2.1.32) was purified 80-fold from the yeast Kluyveromyces lactis induced for this enzyme by growth on lactose. When the purified enzyme was subjected to electrophoresis on an acrylamide gel in the presence of sodium dodecyl sulfate, one protein with an apparent molecular weight of 135,000 was observed. The enzyme has a sedimentation coefficient of 9.6S. This beta-galactosidase and the one from Escherichia coli are not antigenically related. Maximal enzyme activity requires Na+ and Mn2+ and a reducing agent. beta-Galactosidase has Km values of 12 to 17 and 1.6 mM for lactose and o-nitrophenyl-beta-D-galactoside, respectively. The hydrolase and transgalactosylase activities of the enzyme are similar to those of E. coli beta-galactosidase.
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PMID:Purification and properties of an inducible beta-galactosidase isolated from the yeast Kluyveromyces lactis. 3 53

Drosophila melanogaster cell lines Kc and Ca and clones FC and RF6, cultured in vitro, have no detectable beta-galactosidase (beta-galactoside galactohydrolase, EC 3.2.1.23) activity (as measured by hydrolysis of o-nitrophenyl-beta-D-galoctoside). Ecdysterone, a hormonal steroid of critical importance in insect physiology, clearly induces beta-galactosidase activity in D. melanogaster cells cultured in vitro. Induction occurs in cell lines or clones known to be sensitive to ecdysterone (K, Ca, and Fc) and does not occur in clones known to be resistant to the hormone (RF6). Some properties of the hormone-induced beta-galactosidase activity were studied. The Km for o-nitrophenyl galactoside is 0.35 mM and the Ki for lactose is 12 mM (similar to those of Escherichia coli beta-galactosidase); the activity can be recovered after sodium dodecyl sulfate treatment; the enzyme is a tetramer (Mr of the monomer is 64,000).
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PMID:beta-Galactosidase is induced by hormone in Drosophila melanogaster cell cultures. 10 99

Endo-beta-galactosidase, a glycosidase that hydrolyzes Gal beta 1-4 GlcNAc linkages in glycoconjugates, has been used to probe the plasma membrane of human erythrocytes. Coomassie blue staining of stroma components separated by sodium dodecyl sulfate-acrylamide gel electrophoresis indicates that treatment of red cells with endo-beta-galactosidase converts Protein 3, the anion transporter of the erythrocyte, to a more compact staining band. No other components detected by Coomassie staining are affected. Following labeling of red cells with galactose oxidase + NaB3H4, 45 to 50% of the [3H]galactose residues can be released by endo-beta-galactosidase. In contrast, only 5% of the label incorporated by treatment with periodate + NaB3H4, can be removed. [3H]Galactose residues are released from three components: Protein 3, Band 4.5, and the megaloglycolipids. The susceptibility of these components to endo-beta-galactosidase, together with the high content of Gal and GlcNAc present in Protein 3 and the megaloglycolipids, suggests that the erythrocyte membrane contains several components with N-acetyllactosamine repeating units, a structure commonly found in connective tissue glycoconjugates.
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PMID:Effect of endo-beta-galactosidase on intact human erythrocytes. 11 98

We have purified beta-galactosidase and beta-glucuronidase from macrophages of thioglycollate-treated mice using concanavalin A chromatography and immunoprecipitation. The apparent molecular weight of the beta-galactosidase subunit, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, changed during a long term pulse-chase experiment. Following a 1-h pulse with [3H]leucine, radiolabel was present exclusively in an Mr = 82,000 form. However, after a 3-h chase in medium containing unlabeled leucine, most label migrated at Mr = 63,000, and at 24 h, all label was in the Mr = 63,000 form. Electrophoresis of peptides produced by cyanogen bromide cleavage of immunoprecipitates demonstrated structural similarities between precursor and mature forms. A mutation in the mouse, which is known to depress the rate of synthesis of beta-galactosidase in many cell types, proportionately decreased incorporation of [3H]leucine into both the Mr = 82,000 and 63,000 forms. Therefore, by kinetic, structural, and genetic evidence, the large molecular weight beta-galactosidase is a precursor of mature macrophage enzyme. No precursor of the Mr = 75,000 subunit of beta-glucuronidase was detected.
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PMID:Biosynthesis of two lysosomal enzymes in macrophages. Evidence for a precursor of beta-galactosidase. 11 27

A 6-sulfatase specific for sugasr of the galactose configuration was purified 81-fold from the crude extract of Actinobacillus sp. IFO-13310. This preparation contained activity towards both N-acetylgalactosamine 6-sulfate and galactose 6-sulfate (relative activity, 2.4 : 1). The enzyme also release inorganic sulfate from the non-reducing galactose 6-sulfate end group of a trisaccharide disulfate prepared from keratan sulfate by sequential degradation with endo-beta-galactosidase, N-acetylglucosamine-6-sulfatase and exo-beta-N-acetylglucosaminidase. In addition, a tetrasaccharide trisulfate bearing the non-reducing N-acetylglucosamine 6-sulfate end group, also enzymatically prepared from keratan sulfate, was degraded to give rise to inorganic sulfate, N-acetylglucosamine and galactose by the sequential action of this enzyme, N-acetylglucosamine-6-sulfatase, exo-beta-N-acetylglucosaminidase and exo-beta-galactosidase (Charonia lampas).
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PMID:Galactose-6-sulfatase from Actinobacillus sp. IFO-13310 and its action on sulfated oligosaccharides from keratan sulfate. 15 51

A protein, present in bovine seminal plasma, initiates forward motility in immature, immotile caput spermatozoa that have been incubated with a cyclic AMP phosphodiesterase inhibitor. An improved motility assay was developed to study this process and the protein involved. This forward motility protein exhibits multiple forms when fractionated on the basis of charge or molecular weight. Molecular sieving in urea or sodium dodecyl sulfate and dithiothreitol results in a single peak of activity which will re-form the larger aggregates in the absence of these agents. The molecular weight of this monomeric motility protein, as estimated from molecular sieving under these dissociating conditions, is 37,500. The forward motility protein can be partially purified by heat treatment, gell chromatography in urea, and affinity chromatography on concanavalin A/agarose. Enzymatic treatments further suggest a glycoprotein nature, i.e. treatment with beta-galactosidase, neuraminidase, alpha-mannosidase, or galactose oxidase reduces its activity by 50%; treatment with trypsin completely abolishes forward motility protein activity. On the basis of concurrent studies on the activity, properties, and distribution of forward motility protein in bovine body fluids, it is suggested that this protein is involved in the development of the capacity for motility as sperm traverse the epididymis.
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PMID:Bovine sperm forward motility protein. Partial purification and characterization. 21 Nov 30

Strains of Escherichia coli K-12 containing the colicin Ib (Col Ib) factor did not produce progeny phage when infected by T5 bacteriophage. The cells were killed but did not lyse. If sodium dodecyl sulfate (SDS) was added to T5-infected E. coli (Col Ib), lysis occurred prematurely, but no phage were produced. SDS had no effect on infected cells that did not contain the Col Ib factor or on uninfected cells with or without the Col Ib factor. Cells that contained a mutant Col Ib factor that allowed phage production were not prematurely lysed after infection in the presence of SDS. When the Col Ib-containing cells were infected, protein and RNA synthesis stopped at about 10 min postinfection, and the cells released abnormal amounts of 32P-containing material, ATP, and beta-galactosidase into the medium. They also became inhibited in their ability to accumulate thiomethyl-beta-D-galactopyranoside and to utilize glycerol. Two alternative hypotheses are presented to explain these results.
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PMID:Membrane damage in abortive infections of colicin Ib-containing Escherichia coli by bacteriophage T5. 32 28

Escherichia coli Q13 was infected with bacteriophage Q beta and subjected to energy source shift-down (from glucose-minimal to succinate-minimal medium) 20 min after infection. Production of progeny phage was about fourfold slower in down-shifted cultures than in the cultures in glucose medium. Shift-down did not affect the rate of phage RNA replication, as measured by the rate of incorporation of [14C]uracil in the presence of rifampin, with appropriate correction for the reduced entry of exogenous uracil into the UTP pool. Phage coat protein synthesis was three- to sixfold slower in down-shifted cells than in exponentially growing cells, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The polypeptide chain propagation rate in infected cells was unaffected by the down-shift. Thus, the reduced production of progeny phage in down-shifted cells appears to result from control of phage protein synthesis at the level of initiation of translation. The reduction in the rate of Q beta coat protein synthesis is comparable to the previously described reduction in the rate of synthesis of total E. coli protein and of beta-galactosidase, implying that the mechanism which inhibits translation in down-shifted cells is neither messenger specific nor specific for 5' proximal cistrons. The intracellular ATP pool size was nearly constant after shift-down; general energy depletion is thus not a predominant factor. The GTP pool, by contrast, declined by about 40%. Also, ppGpp did not accumulate in down-shifted, infected cells in the presence of rifampin, indicating that ppGpp is not the primary effector of this translational inhibition.
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PMID:Control of protein synthesis in Escherichia coli: control of bacteriophage Q beta coat protein synthesis after energy source shift-down. 38 18

The apparent low level of synthetic substrate beta-D-galactosidase activity in liver from patients with the Hurler-Hunter syndrome is caused by the inhibitory effect of accumulated glycosaminoglycans. We have demonstrated complete inhibition of GM1 ganglioside beta-galactosidase activity in vitro by both heparan sulfate and dermatan sulfate, but the effect on lactosylceramide and galactosylceramide hydrolysis was less marked. In contrast, lysosomal neuraminidase activity in vitro was enhanced by the addition of glycosaminoglycans. These observations are discussed in relationship to the observed storage pattern of glycosphingolipids in liver from patients with mucopolysaccharidoses.
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PMID:The effect of glycosaminoglycans on the in vitro activity of human skin fibroblast glycosphingolipid beta-galactosidases and neuraminidases. 40 73


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