Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hamster pouch buccal epithelium (HPBE) was isolated and grown in primary cultures on rat-tail collagen-coated growth surfaces. The cultured pouch buccal epithelium (CPBE) was characterized morphologically with electron microscopy as stratified multilayers of epithelial cells with well-developed tonofibrillar-desmosomal complexes. Only the superficial layer of the cultured cells exhibited evidence of terminal differentiation. Alkaline phosphatase, alcohol dehydrogenase, and aminopeptidase activities in the primary cultured cells were determined by biochemical assays and found to be similar to those of homogenates of freshly excised hamster pouch epithelium. In addition, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS PAGE), keratins and total proteins associated with the cultured cells were similar to those of freshly excised HPBE. The permeability characteristics of the cultured cells was determined by placing cultured cells grown on permeable polycarbonate disks in a Side-Bi-Side diffusion apparatus and quantitating the transcellular flux of tritium-labeled water, fluorescein, and fluorescein isothiocyanate dextrans (MW 3800 to 150,000). The cultured cells were least permeable on the third day of culture and were not permeable to substances with a MW greater than about 18,000. Our results indicate that primary cultures of hamster pouch epithelium exhibit biochemical properties similar to those of the excised hamster pouch epithelium from which they were derived. The morphological and permeability characteristics of cultured hamster epithelium were similar to those of nonkeratinized stratified oral epithelia typical of buccal mucosa in man, rabbit, and other species. CPBE, as described here, represents a potentially useful tool for in vitro drug transport, metabolism, pharmacology, and toxicology studies.
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PMID:Cultured buccal epithelium: an in vitro model derived from the hamster pouch for studying drug transport and metabolism. 247 7

++Post-alcoholic lesion of liver, pancreas, and heart muscle was estimated by measurement of some enzymes activity. Alcoholic in-patients were divided into two groups in regard to the age and the length of the disease. The activity of enzymes in the blood was measured by kinetic methods using the RA-1000/Technicon analyser. It was shown that the increase of activity of alanine aminotransferase (AlAT), gamma-glutamyltransferase (GGTP), and alcohol dehydrogenase (ADH) may indicate the ++post-alcoholic liver damage, while increase of activity of alpha-+-amylase and ++leucine aminopeptidase (LAP) may be useful for the diagnosis of pancreas lesion, and creatine kinase (CK) as well as lactate dehydrogenase (LDH) for the evaluation of postalcoholic lesion of the heart muscle.
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PMID:[Enzymatic diagnosis of alcoholism-induced damage of internal organs]. 257 12

Parameters for the zinc ion have been developed in the self-consistent charge density functional tight-binding (SCC-DFTB) framework. The approach was tested against B3LYP calculations for a range of systems, including small molecules that contain the typical coordination environment of zinc in biological systems (cysteine, histidine, glutamic/aspartic acids, and water) and active site models for a number of enzymes such as alcohol dehydrogenase, carbonic anhydrase, and aminopeptidase. The SCC-DFTB approach reproduces structural and energetic properties rather reliably (e.g., total and relative ligand binding energies and deprotonation energies of ligands and barriers for zinc-assisted proton transfers), as compared with B3LYP/6-311+G** or MP2/6-311+G** calculations.
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PMID:Modeling zinc in biomolecules with the self consistent charge-density functional tight binding (SCC-DFTB) method: applications to structural and energetic analysis. 1263 71

Maize aminopeptidase is coded by four genes. Amp1 and Amp2 have been localized to chromosome 1. A three-point cross shows the gene order to be Amp2-15%-Amp1-33%-Adh2 (alcohol dehydrogenase). Amp3 and Amp4 assort independently of each other and of chromosome 1 aminopeptidases. Another linkage relationship among the maize genes Amy2 (amylase), Cat1 (catalase), and Amp3 exists, but the chromosome location has yet to be established unequivocally.
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PMID:Genetic Control and Linkage Relationships among Aminopeptidases in Maize. 1724 24

Enzyme electrophoresis was used to compare the isozyme phenotypes of Oryza sativa, IR31917 (AA genome), and two O. minuta accessions (Om 101089 and Om101141; BBCC genome) for ten enzyme systems. Between the two species, two systems were monomorphic (isocitrate dehydrogenase and alcohol dehydrogenase) and eight were polymorphic (shikimate dehydrogenase, phosphogluconate dehydrogenase, phosphoglucose isomerase, malate dehydrogenase, glutamate oxaloacetate transaminase, esterase, aminopeptidase, and endopeptidase). Polymorphism between O. minuta accessions was detected for shikimate dehydrogenase and glutamate oxaloacetate. As expected, the quaternary structure of the O. minuta isozymes was comparable to that of O. sativa. Possible allelic relationships with known O. sativa alleles and their genomic designation are discussed. Combined with chromosome data, the interspecific variation was exploited to monitor the relative genetic contribution of the two parents in the IR31917/Om101141 F1 hybrids and recurrent (IR31917) backcross progenies. The isozyme content of F1 hybrid reflected its triploid nature (ABC genome composition), while that of the backcross progenies paralleled the duplication of the A genome and the gradual loss of O. minuta chromosomes during the backcrossing process. Evidence is provided for a degree of homoeology between the A, B, and C genomes, and for introgression from O. minuta into O. sativa.
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PMID:Comparative studies of isozymes in Oryza sativa, O. minuta, and their interspecific derivatives: evidence for homoeology and recombination. 2419 Mar 57