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)

Cell differentiation during spermatogenesis in the rat has been analyzed in terms of the formation of specific "marker" enzymes. Hyaluronidase and other acrosomal enzymes are formed in spermatids according to a highly predictable time schedule which may be termed a "molecular biological clock". The acrosomal enzymes beta-galactosidase and N-acetyl-beta-glucosaminidase exist as isoenzyme forms distinct from enzymes with similar substrate specificities in the lysosomes of precursor cells. Differentiation of spermatids thus involves the loss of gene expression for lysosomal enzymes and the activation of genes for acrosomal isoenzymes. Spermatogenesis is characterized by the sequential loss of expression of many genes, as evidenced by the loss of beta-glucuronidase in the differentiation of spermatogonia to spermatocytes, and the loss of uridine diphosphatase activity in the differentiation of spermatocytes to spermatids. The apparent absence of ornithine decarboxylase activity from spermatids suggests a dependence of these cells upon Sertoli cells for the provision of putrescine and/or spermidine. Such biochemical cooperativity among germinal cells may be necessary as the genes of spermatids are repressed and late spermatids become metabolically inactive. Spermatogenesis is also characterized by changes in the cellular content and rates of synthesis and phosphorylation of specific acidic chromatin proteins. It is hypothesized that these proteins may participate in the activation or repression of genes during spermatogenesis.
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PMID:Gene activation during spermatogenesis. 112 12

The nucleotide sequence was determined for a 3-kilobase genomic fragment containing the ornithine decarboxylase gene of Saccharomyces cerevisiae. The fragment contained two open reading frames. Gene disruption localized the ornithine decarboxylase gene to a 1398-nucleotide open reading frame. Transcription of the yeast gene initiated at several sites 171 to 211 nucleotides 5' of the translational start site. The 3' end of the transcript extended approximately 300 nucleotides beyond the end of the ornithine decarboxylase coding region and contained two copies of the yeast ARS core sequence. Translation of the ornithine decarboxylase gene appeared to initiate at the first AUG condon of the open reading frame based upon translational fusions with the Escherichia coli beta-galactosidase gene. Since no introns were apparent, the 1398-nucleotide open reading frame was predicted to encode a 466-amino acid protein with a calculated Mr = 52,369. The deduced protein differed significantly in size from previous reports on yeast ornithine decarboxylase, but was very similar in size to mammalian ornithine decarboxylase. When the predicted amino acid sequence of yeast ornithine decarboxylase was compared with that of the mouse enzyme, alignment of the sequences revealed that 40% of the amino acid residues were identical. Chou-Fasman predictions of the secondary structure of the two enzymes indicated that secondary structure was also highly conserved.
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PMID:The gene and the primary structure of ornithine decarboxylase from Saccharomyces cerevisiae. 303 69

The biochemical properties of 39 strains of Haemophilus avium from chickens were determined. All the strains produced acid from fructose, galactose, glucose and mannose but not from lactose. Variable reactions were found for arabinose, maltose, mannitol, sorbitol, trehalose and xylose. No strains showed urease activity or produced indole, while beta-galactosidase and/or ornithine decarboxylase activity was present in some strains. This variability allowed the recognition of 15 biochemical biovars including some not previously recognized in H. avium. Only 25 (64%) of the H. avium strains could be assigned to the three species (Pasteurella avium, P. volantium and Pasteurella species A) recently proposed to replace H. avium.
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PMID:Biochemical properties of catalase-positive avian haemophili. 315 Dec 6

The PathoTec "Rapid I-D System" and two experimental test strips for ornithine decarboxylase and beta-galactosidase have been evaluated for accuracy and ability to identify 1,252 members of the Enterobacteriaceae obtained from fresh clinical specimens. Accuracy of identification with the commercially available test system was 94.7%; this level increased to 98.5% with the addition of the two experimental test strips. Average individual accuracy of the 12-strip test system on a side-by-side basis with similar conventional procedures was 98%. In addition, 103 gram-negative nonfermentors were accurately grouped. The PathoTec System was applicable to 95% of the primary isolation plates used and provided biochemical data within 4 h after inoculation. The conventional test procedures were applicable to 100% of the primary isolation plates used and produced data within 48 h.
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PMID:Evaluation of the PathoTec "Rapid I-D System" and two additional Experimental reagent-impregnated paper strips. 458 97

The Analytab system of 20 biochemical tests for identification of Enterobacteriaceae was evaluated in parallel with conventional tests on 128 Enterobacteriaceae, 5 Aeromonas, and 1 Yersinia enterocolitica. The results of tests for H(2)S and indole production, citrate utilization, lysine and ornithine decarboxylase, arginine dihydrolase, nitrate reduction, beta-galactosidase, and fermentation of arabinose, rhamnose, mannitol, and glucose showed almost complete agreement between the two systems. Eighty-eight per cent of Enterobacteriaceae were correctly speciated with the Analytab system; on repeat testing with heavier inocula of organisms failing to ferment glucose initially, the proportion of Enterobacteriaceae correctly speciated became 93%.
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PMID:Evaluation of accuracy of multitest micromethod system for identification of Enterobacteriaceae. 494 Aug 67

The time courses of changes of three enolase isozymes (alpha alpha, alpha gamma, and gamma gamma), S-100 protein, 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase), ornithine decarboxylase (ODC), beta-galactosidase, and glucose-6-phosphate dehydrogenase (G6PDH) were examined from 1 to 14 days after cutting of the preganglionic nerve (denervation) or the postganglionic nerve (axotomy) of the superior cervical sympathetic ganglion (SCG) of the rat. The wet weight and protein content in the axotomized SCG increased continuously, to nearly twice those of the denervated SCG for 1-2 weeks after the operations. Among enolase isozymes in the SCG, neuron-specific gamma gamma-enolase decreased rapidly after denervation and stayed at a low level for 2 weeks, whereas the isozyme remained almost unchanged after axotomy. On the contrary, ganglionic alpha alpha-enolase and the alpha gamma-hybrid form increased remarkably to reach a maximum at the second day after axotomy, and remained above control for 1 to 2 weeks; these two enolase isozymes showed little change after denervation. Denervation caused a much larger increase than did axotomy in the ganglionic S-100 protein, an astrocyte-specific protein, during the first week after the operation, while the protein content decreased after 2 weeks of either denervation or axotomy. CNPase, a myelin-associated enzyme, rose suddenly 2 days after axotomy, and remained at a rather high level compared with the denervated ganglion, which showed little variation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of denervation and axotomy on nervous system-specific protein, ornithine decarboxylase, and other enzyme activities in the superior cervical sympathetic ganglion of the rat. 631 94

We examined the gene expression of the Escherichia coli cad operon, which consisted of the genes cadB and cadA (lysine decarboxylase), using cells possessing cadB-lacZ fusion gene. The cad operon was expressed when O2 was limited, and the expression was optimal at pH 6.3. The beta-galactosidase activity was lowered by the addition of sodium carbonate to the medium. The expression of the cad operon was reduced in cells containing the plasmid-encoding ornithine decarboxylase, which produced carbon dioxide, indicating that the gene expression of the cad operon was regulated by carbon dioxide (or its derivatives). It is known that the Krebs cycle is a major pathway for producing carbon dioxide, and that its activity is repressed when O2 is limited. Thus, our present results suggested that the physiological role of the cad operon is to supply carbon dioxide when its internal level is lowered under O2-limiting conditions at a low pH.
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PMID:Escherichia coli cad operon functions as a supplier of carbon dioxide. 802 68

Since the speF-potE operon (pPT71 clone) encoding inducible ornithine decarboxylase (iODC) and polyamine transport potE protein is inducible at acidic pH, a gene encoding a protein involved in the enhancement of expression of the operon was searched for. Using the fused gene containing the upstream sequence of the speF-potE operon and the open reading frame of beta-galactosidase as a reporter gene, a clone (pPTS23) which causes the increase of beta-galactosidase activity at acidic pH was isolated. The clone also increased iODC activity at acidic pH and was identified as a gene encoding RNase III. This is the first example that RNase III increases the translational efficiency of mRNA derived from Escherichia coli gene by cutting the 5'-untranslated region of mRNA.
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PMID:Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein. 816 35

Transcriptional activation studies involving the human oncoprotein and transcription factor Myc and its helix-loop-helix partner protein Max in mammalian cells are critical due to the presence of endogenous Myc and Max proteins. Here we show that co-expression of the human c-myc and max genes from 2micro circle derived high copy number vectors in yeast cells stimulate the transcriptional activation of a LacZ reporter gene fused to the yeast cytochrome-c1 oxidase minimal promoter containing the adenovirus major late promoter element (AMLPE). The exchange of the single Myc binding site in the AMLPE by the two E-box DNA motifs (CACGTG) present in the Myc responsive element of a human Myc target gene (ornithine decarboxylase) in front of a promoter-reporter gene cassette results in a two-fold enhanced beta-galactosidase expression. Low expression of max and high level expression of c-myc at the same time led to a further enhancement of transcriptional activation from this promoter-reporter gene cassette.
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PMID:Control of the Myc-Max mediated transactivation in yeast by natural promoter elements. 909 Jan 24

Because arginase hydrolyzes arginine to produce ornithine and urea, it has the potential to regulate nitric oxide (NO) and polyamine synthesis. We tested whether expression of the cytosolic isoform of arginase (arginase I) was limiting for NO or polyamine production by activated RAW 264.7 macrophage cells. RAW 264.7 cells, stably transfected to overexpress arginase I or beta-galactosidase, were treated with interferon-gamma to induce type 2 NO synthase or with lipopolysaccharide or 8-bromo-cAMP (8-BrcAMP) to induce ornithine decarboxylase. Overexpression of arginase I had no effect on NO synthesis. In contrast, cells overexpressing arginase I produced twice as much putrescine after activation than did cells expressing beta-galactosidase. Cells overexpressing arginase I also produced more spermidine after treatment with 8-BrcAMP than did cells expressing beta-galactosidase. Thus endogenous levels of arginase I are limiting for polyamine synthesis, but not for NO synthesis, by activated macrophage cells. This study also demonstrates that it is possible to alter arginase I levels sufficiently to affect polyamine synthesis without affecting induced NO synthesis.
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PMID:Arginase I: a limiting factor for nitric oxide and polyamine synthesis by activated macrophages? 1108 91


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