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)

Marine mussels secrete the byssus in order to attach to solid surfaces and to survive under the turbulent effects of waves. The adhesive responsible for this attachment is the polyphenolic protein secreted by the phenol gland in the foot of the animal. To purify this adhesive protein from the chilean mussel Mylilus chilensis, a modification of previous procedures has been developed. Accordingly, the protein is differentially precipitated with acetone in the presence of 0.25 N HCl. The purified protein is rich in the amino acids lysine, 3,4-dihydroxyphenylalanine, serine, threonine, proline and hydroxyproline. The protein exhibited strong adhesion to glass and other solid supports. Moreover, it has been found that the adhesive protein can mediate the immobilization of beta-galactosidase to glass. About 75% of the enzyme activity was immobilized under the experimental conditions described. This is the first study reporting the use of the polyphenolic protein to immobilize enzymes.
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PMID:Bioadhesives: a biotechnological opportunity. 213 19

N-Methyl-4-phenylpyridinium ion (MPP+) was found to be accumulated in human melanoma cell lines, HMV-I and -II, which originate from human melanoma and differentiate into subclones, HMV-I and -II. HMV-II cells can produce a large amount of melanin, while the other cells produce less. After 3 day culture of these cells in the presence of 1-100 microM MPP+, MPP+ was accumulated in both types of cells and a much larger amount of MPP+ was accumulated in melanin-rich HMV-II cells than in HMV-I cells, even though the uptake velocity of MPP+ into both types of cells was almost the same. In addition, both types of cells could survive, even with MPP+ accumulation. Protein amounts, a non-specific enzyme, beta-galactosidase activity, and intracellular DOPA concentrations in both types of cells, were not affected by the presence of MPP+. These results suggest that MPP+ is accumulated in non-dopaminergic cells and the accumulation is enhanced by the presence of melanin.
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PMID:Accumulation of N-methyl-4-phenylpyridinium ion (MPP+) in human melanoma cell line, HMV-I and -II. 313 52

Aromatic L-amino acid decarboxylase (AADC) decarboxylates L-DOPA and 5-hydroxytryptophan into dopamine and serotonin, respectively. Starting from a rat AADC cDNA clone isolated in our laboratory, we produced a beta-galactosidase-AADC fusion protein in E. coli. It was purified from inclusion bodies and injected into a rabbit. The antiserum identified AADC on a Western blot of extracts from rat organs as a unique 50 kDa band; it also strongly reacted by immunohistochemistry with dopaminergic and serotonergic neurons. This new beta-galactosidase-AADC fusion protein then constitutes a useful tool for producing AADC as an antigen free of contamination by mammalian proteins.
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PMID:Preparation of an antiserum using a fusion protein produced by a cDNA for rat aromatic L-amino acid decarboxylase. 851 Aug 30

The tyrosine hydroxylase (TH) gene is expressed exclusively in cells and neurons that synthesize and release L-DOPA or catecholamines. To further understand the molecular genetic mechanisms that regulate this cell-type specific expression, a chimeric gene was prepared by linking 3.6 kb of the 5' flanking DNA of the mouse TH gene, including the +1 initiation site for transcription, to an E. coli beta-galactosidase reporter. This fusion gene (TH3.6LAC) was used to prepare transgenic mice, and the tissue distribution of expression of TH3.6LAC was determined by the measurement of beta-galactosidase enzymatic activity and/or by the detection of the transcription product of the chimeric gene by RNase protection assays. In two separate founder lines, TH3.6LAC expression was observed in every region of the brain that was examined, including the olfactory bulb, brainstem, cerebellum, diencephalon, hippocampus, striatum, and cerebral cortex. Expression of TH3.6LAC was observed in the adrenal gland of one founder line but not in the other. TH3.6LAC activation was undetectable in peripheral organs that were examined, including the liver, heart, salivary gland, kidney, lung, and spleen. Although 3.6 kb of the 5' regulatory DNA of the mouse TH gene is sufficient to activate the TH fusion gene in the mouse, it is not enough to restrict its expression to catecholaminergic cells.
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PMID:3.6 kb of the 5' flanking DNA activates the mouse tyrosine hydroxylase gene promoter without catecholaminergic-specific expression. 852 54

Dopamine is an important signaling molecule in the nervous system; it also plays a vital role in the development of diverse non-neuronal tissues in the fruit fly Drosophila melanogaster. The current study demonstrates that males depleted of dopamine as third instar larvae (via inhibition of the biosynthetic enzyme tyrosine hydroxylase) demonstrated abnormalities in courtship behavior as adults. These defects were suggestive of abnormalities in sensory perception and/or processing. Electroretinograms (ERGs) of eyes from adults depleted of dopamine for 1 day as third instar larvae revealed diminished or absent on- and off-transients. These sensory defects were rescued by the addition of L-DOPA in conjunction with tyrosine hydroxylase inhibition during the larval stage. Depletion of dopamine in the first or second larval instar was lethal, but this was not due to a general inhibition of proliferative cells. To establish that dopamine was synthesized in tissues destined to become part of the adult sensory apparatus, transgenic lines were generated containing 1 or 4 kb of 5' upstream sequences from the Drosophila tyrosine hydroxylase gene (DTH) fused to the E. coli beta-galactosidase reporter. The DTH promoters directed expression of the reporter gene in discrete and consistent patterns within the imaginal discs, in addition to the expected expression in gonadal, brain, and cuticular tissues. The beta-galactosidase expression colocalized with tyrosine hydroxylase protein. These results are consistent with a developmental requirement for dopamine in the normal physiology of adult sensory tissues.
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PMID:Dopamine and sensory tissue development in Drosophila melanogaster. 1135 39