Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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 study deals with the distribution of acid and alkaline phosphatases, ATPase, 5-nucleotidase, nonspecific esterase, specific cholinesterase, and beta-galactosidase in the diencephalon of the frog. The highlights of the present study are the following: i) Acid phosphatase is present in all the neurons, whereas the tracts and commissures are completely negative. ii) Most of the tracts and commissures are positive for 5-nucleotidase. This confirms the author's previous findings that the tracts and commissures of all the areas of frog brain are intensely positive for 5-nucleotidase. iii) beta-galactosidase activity in the nuclei of the diencephalon is either mild or completely absent, whereas the commissures and tracts show positive activity. iv) Habenulothalamic connections are intensely positive for specific cholinesterase and non-specific esterase, moderately positive for beta-galactosidase and completely negative for other enzymes. v) The epiphysis (pineal organ) shows intense reaction for adenosine triphosphatase, acid phosphatase, and 5-nucleotidase and moderate reaction for alkaline phosphatase and non-specific esterase. In contrast to the above enzymes, the specific cholinesterase and beta-galactosidase are completely missing. vi) Lateral forebrain bundles are completely negative for all the enzymes except alkaline phosphatase and beta-galactosidase. The distribution of these enzymes has been correlated with the functional aspects of various nuclei, tracts, and commissures of the diencephalon of the frog.
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PMID:The chemoarchitectonics of the diencephalon of frog (Rana tigrina). 15 81

The distributions of acid and alkaline phosphatases, 5-nucleotidase, ATPase, non-specific esterase, specific cholinesterase, succinic dehydrogenase and beta-galactosidase are described in the mesencephalic auditory, tegmental and cranial nerve nuclei of the frog (Rana tigrina). The main results of the study are as follows: The laminar, principal, and magnocellular nuclei of the torus semicircularis, which are associated with auditory functions, show intense activity of specific cholinesterase. On the other hand, the commissural and subependymal mid-line nuclei, whose functions are doubtful, show a complete lack of this enzyme. The nucleus isthmi shows intense acid phosphatase, ATPase, non-specific esterase, specific cholinesterase and succinic dehydrogenase activities. Non-specific esterase is virtually absent from all the areas studied except the nucleus isthmi and the 3rd and 4th cranial nerve nuclei. Most of the commissures and fibre tracts show intense activity for beta-galactosidase and 5-nucleotidase. The possible roles of these enzymes in glycolipid and myelin metabolism are discussed.
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PMID:Histoenzymological analysis of mesencephalic auditory, tegmental and cranial nerve nuclei in the frog (Rana tigrina). 21 17

The effects of age-specific peculiarities and the duration of maintaining rats on a ration with 4 per cent of protein (the initial mass of rats in the 1st group 100 g each; duration of the experiment--30 days. Initial mass rats in the 2d group--200 g each; duration of experiment--90 days on the activity of the lysosomal hydrolase was studied. The latter included beta-glucosidase, beta-galactosidase, beta-glucoronidase, beta-N-acetylglucosaminidase, arylsulfatase A and B, acid phosphatase, phospholipase A1 and A2, cholinesterase, the total proteolytic activity and that of catepsines A, B, C and D. An ambiguity of changes in the enzymes activity in the animals of the 1st and 2d groups was revealed. Placing the growing animals on a ration containing 4 per cent of protein produces an activation of the most of the lysosomal enzymes, whereas in animals of the 2d test group the nature of changes in the activity of individual enzymes proved to differ quite appreciably. Thus, the summary activity of catepsines, beta-glucoronidase and cholinesterase was below the control level, while the activity of beta-galactosidase, beta-N-acetyl-glucoseaminidase and phospholipase A1 and A2 went up. A prolonged maintenance of rats on a protein-poor ration led to upsetting the stability of the lysosomal membranes, which manifested itself in a higher solubilization of lysosomal enzymes in vitro.
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PMID:[Characteristics of the enzymatic adaptation of rat liver lysosomes to protein deficiency]. 68 19

The origin and properties of cytosolic neuraminidase (acylneuraminyl hydrolase, EC 3.2.1.18) from pig brain were studied. 1. The brain extracts containing the cytosol derived from neuronal bodies and glial cells carry 0.69 munits neuraminidase/g fresh tissue. The behaviour of neuraminidase during extraction closely paralleled that of authentic cytosolic enzyme, lactate dehydrogenase; whereas, it differed from that of the lysosomal enzymes, beta-hexosaminidase and beta-galactosidase, also found in the extracts. 2. Nerve endings from either crude or purified preparations, when treated by hypoosmotic shock, released neuraminidase activity up to a maximum of 1.25 munits/g fresh tissue. The behaviour of releasable neuraminidase was always identical to that of lactate dehydrogenase and very similar to that of ATPase and acetylcholinesterase. Typical lysosomal enzymes, however, such as beta-galactosidase and beta-hexosaminidase, behaved differently under the same conditions. This neuraminidase activity is thought to be derived from the cytosol of nerve endings. 3. The specific activity of neuraminidase in nerve-ending cytosol is 15--20 times that in neuronal body and glial cell cytosol. Some properties (pH, Km value, V/t relationship) of the cytosolic enzymes of different origin are similar; others (stability on standing at 4 degrees C; resistance to freezing and thawing) are different. Hypoionic solutions caused both cytosolic neuraminidases to slowly precipitate and to assume a stable insoluble form which was still active.
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PMID:Studies on brain cytosol neuraminidase. II. Extractability, solubility and intraneuronal distribution of the enzyme in pig brain. 71 57

We have obtained transgenic mice expressing nuclearly targeted beta-galactosidase (nls-beta-gal) under the control of a chicken acetylcholine receptor alpha-subunit promoter. The expression of the transgene was detected in early somites, starting before embryonic day 9.5. In 13-day embryos, the expression pattern of the transgene closely paralleled that of the endogenous mouse alpha-subunit gene, assessed by in situ hybridization. Our results illustrate, with single-cell resolution, the tissue specificity of this alpha-subunit promoter during embryogenesis. After birth, the overall beta-galactosidase activity rapidly decreased with age. However, in diaphragms of newborn animals, beta-galactosidase activity selectively persisted in nuclei underlying the motor endplates. The latter were revealed by an acetylcholinesterase stain. Nls-beta-gal was also visualized by indirect immunofluorescence, while endplates were labelled with fluorescent alpha-bungarotoxin. Confocal microscopy unambiguously identified the more intensely stained nuclei as synaptic 'fundamental nuclei', and allowed estimates of relative staining levels. Thus an 842 bp acetylcholine receptor gene promoter confers preferential synaptic expression to a reporter gene within myofibres in vivo.
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PMID:An acetylcholine receptor alpha-subunit promoter conferring preferential synaptic expression in muscle of transgenic mice. 190 Apr 67

The phototoxicities of six metalloporphyrin dimethylesters (i.e. cobalt (Co), copper (Cu), manganese (Mn), nickel (Ni), tin (Sn) and zinc (Zn) were investigated. Hemolysis of human erythrocytes and inactivation of two enzymes (acetylcholinesterase and beta-galactosidase) were used to assess the phototoxic efficacy of these metal chelates. Tin protoporphyrin (SnPP), the only porphyrin found to hemolyze erythrocytes at a concentration of 40 microM (radiation dose, 230 kJ m-2), was much less efficient than either free protoporphyrin IX or hematoporphyrin. SnPP completely inactivated beta-galactosidase at concentrations above 15 microM (radiation dose, 75 kJ m-2) and drastically interfered with acetylcholinesterase activity at a concentration of 150 microM (radiation dose, 75 kJ m-2). CoPP, CuPP, MnPP, NiPP and ZnPP were ineffective photohemolytic agents at 40 microM (radiation dose, 230 kJ m-2), but inactivated acetylcholinesterase and beta-galactosidase activity to varying degrees. These results suggest that (i) metal ions reduce the phototoxicity of protoporphyrin IX, (ii) different metal ions reduce the phototoxic activity of protoporphyrin IX to different degrees and (iii) the biological activities of the various metal complexes vary in different assay systems.
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PMID:Metalloporphyrin phototoxicity. 212 21

Nicotinic acetylcholine receptors (nAChR) are found both in vertebrate and insect central nervous systems. We have isolated a Drosophila gene by crosshybridization with a vertebrate probe. Structural conservation of domains of the deduced protein and of intron/exon boundaries indicate that the Drosophila gene encodes an nAChR alpha-like subunit (ALS). That the Drosophila gene product most resembles the neuronal set of vertebrate nAChRs alpha-subunits is also indicated by the failure of an ALS-beta-galactosidase fusion protein to bind alpha-bungarotoxin on blots in contrast to vertebrate endplate alpha-subunit constructions. The ALS encoding gene exceeds 54 kb in length and the transcript has a very long and unusual 5' leader. As we found previously for a gene whose product is also involved in cholinergic synapses, acetylcholinesterase, the leader encodes short open reading frames, which might be involved in translation control. We also note the presence of opa repeats in the gene, as has been found for various Drosophila genes expressed in the nervous system.
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PMID:Conservation of neural nicotinic acetylcholine receptors from Drosophila to vertebrate central nervous systems. 284 Feb 81

Radiation inactivation is a method to determine the apparent target size of molecules. In this report we examined whether radiation inactivation of various enzymes and brain receptors is influenced by the preparation of samples preceding irradiation. The apparent target sizes of endogenous acetylcholinesterase and pyruvate kinase from rat brain and from rabbit muscle and benzodiazepine receptor from rat brain were investigated in some detail. In addition the target sizes of alcohol dehydrogenase (from yeast and horse liver), beta-galactosidase (from Escherichia coli), lactate dehydrogenase (endogenous from rat brain), and 5-HT2 receptors, acetylcholine muscarine receptors, and [35S] butyl bicyclophosphorothionate tertiary binding sites from rat brain were determined. The results show that apparent target sizes are highly influenced by the procedure applied for sample preparation before irradiation. The data indicate that irradiation of frozen whole tissue as opposed to lyophilized tissue or frozen tissue homogenates will estimate the smallest and most relevant functional target size of a receptor or an enzyme.
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PMID:The apparent target size of rat brain benzodiazepine receptor, acetylcholinesterase, and pyruvate kinase is highly influenced by experimental conditions. 284 37

The activities of acid phosphatase, hexosaminidase, beta-galactosidase, Mg2+-stimulated Na+K+ATPase, fumarase and ATP:citrate lyase were measured in grey matter of rabbit spinal cord 7-8 days after intra-ventricular or intra-cisternal injection of aluminium. RNA, DNA, and water content were measured in whole spinal cords. Choline acetyltransferase (CAT) and acetylcholinesterase were assayed in dorsal grey matter of the cord, which contained no aluminium-induced neurofilament accumulations (NFAs), and ventral grey matter, which had large numbers of such NFAs. CAT was also assayed in the hypoglossal nerve. None of these measures were consistently altered in the aluminium treated rabbits, although the activity of beta-galactosidase was increased in the NFA-free caudate nucleus of rabbits given aluminium intra-ventricularly, possibly due to the presence of phagocytes on the ventricular surface of the caudate. It is concluded that neither aluminium nor its induced NFAs has a gross effect on neuronal metabolism within 7-8 days.
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PMID:Biochemical studies on rabbits with aluminium induced neurofilament accumulations. 298 21

The authors presented the results of a study of enzymuria (cholinesterase, gamma-glutamine transferase, alkaline phosphatase, beta-galactosidase and lactate dehydrogenase with separate determination of N- and M-subunits) in 20 patients with a mixed form of glomerulonephritis (GN), 36 with the nephrotic form of GN and 13 patients with the hematuric form of GN. The clinical importance of the determination of enzymatic activity in the urine in GN of children lies in the recognition of the degree of damage of the glomerular filter as well as the nephrothelium. Basing on enzymuria pathophysiological syndromes found in various combinations in the above forms of GN were identified. Three degrees of damage of the permeability of the glomerular filter were defined for high molecular proteins. Differences in individual values of the activity of some enzymes gave rise to differential-diagnostic coefficients as well as differential-diagnostic tables which could be used for differential diagnosis between the GN mixed and nephrotic forms.
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PMID:[Clinical significance of enzymuria in glomerulonephritis in children]. 376 57


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