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)

The histrochemistry of the adrenal glands was studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). It was impossible to demonstrate any reactivity to UDPG-GT, ADH, alanyl aminopeptidase, leucine aminopeptidase, xilitol (NAD-dependent) dehydrogenase, beta-glucuronidase and aryl-sulfatase in these glands. Total phosphorylase was found in scattered cells of the glomerulosa and adjacent outer fasciculata of one C. penicillata. The dehydrogenases (LDH, G-6-PDH,6-PGDH, NADPH2-TR,ICDH,SDH,NADH2-TR, alpha-GPDH, beta-OHBDH) as well as the hydrolases (except alkaline phosphatase, ATPase, and acetylcholinesterase) showed a stonger reactivity in the cortical part. Some hydrolases (naphthol acetate esterase, acid phosphatase) and cytochrome oxidase were less reactive in the zona glomerulosa, where the dehydrogenases were more abundant. The outer fasciculata and the reticularis also showed a strong dehydrogenase reactivity.
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PMID:Histochemical studies on the adrenal glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 0 44

The histochemistry of the neural cells was studied in the submandibular ganglia of 5 Callithrix jacchus (3 males and 2 females) and 4 Callithrix penicillata (2 males and 2 females). These cells contain neutral mucopolysaccharides, nucleoproteins and lipidic materia, but are apparently devoid of glycogen. It is impossible to demonstrate in them any reactivity for UDPG-GT, phosphorylases, ATPase at pH 6.3, leucine aminopeptidase and alanyl aminopeptidas. The reaction for the other searched enzymes was as follows: weak (F-1,6-P Ald and cytochrome oxidase), weak to moderate (ADH, 6-P-GDH, ICDH, SDH, MDH, alpha-GPDH and beta-OHBDH), moderate (G-6-PDH, F-1,6-PA, LDH and GDH), moderate to strong (ATPase at pH 7.4, nonspecific esterase and acid phosphatase) and strong (G-6-PA, NADH2,-TR, NADPH2-TR, ATPase at pH 8.5 and 9.4 and alkaline phosphatase).
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PMID:Histochemical studies on the submandibular ganglia of marmosets (Callithrix jacchus and Callithrix penecillata). 14 13

The epithelial cells in the taste buds of C. jacchus and C. penicillata show a moderate amount of ribonucleic acid an a concentration of a PAS-positive diastase-resistant material at their apical part. These cells are devoid of UDPG-GT, phosphorylases, G-6-PA, alanyl aminopeptidase, leucine aminopeptidase, cholinesterase and MAO; they present a weak reaction of F-1, 6-P Ald, LDH, SDH, MDH, cytochrome oxidase, beta-OHBDH, nonspecific esterase and acid phosphatase and a stronger reaction to ADH, NADPH2-TR, ATPases, alpha-GPDH, alkaline phosphatase, 5-nucleotidase and GDH. Although some enzymes (alkaline phosphatase, 5-nucleotidase and ATPases) have an almost uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller uniform reactivity by the several taste buds, the other ones react with a lesser intensity in the smaller taste buds of the fungiform papillae. As a rule the apical part of the cells shows a stronger enzymatic reactivity. The taste buds of the marmosets are penetrated by acetylcholinesterase positive nerve fibers whereas the autonomic ganglia in the connective tissue contain both-acetyl and butyrylcholinesterase.
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PMID:Histochemical observations on the taste buds of the marmosets (Callithrix jacchus and Callithrix penicillata). 15 39

The technique of differential scanning calorimetry (DSC) has been applied to the study of temperature-induced irreversible denturation and thus to the heat stability of soluble and Sepharose-bound liver alcohol dehydrogenase (LADH, EC 1.1.1.1) and lactate dehydrogenase (LDH, EC 1.1.1.27) in the presence of various coenzymes or coenzyme fragments. The transition temperature (Ttr) of 82.5 degrees C obtained for soluble LADH was increased by 12.5 degrees C in the presence of a saturating concentration of NACH. In the presence of NAD+, Ttr increased by 8.5 degrees C, whereas ADP-ribose and AMP caused an increase in Ttr of only 2 and 1 degree C, respectively. The Ttr of 85.5 degrees C obtained for Sepharose-bound LADH was increased by about 12 degrees C after the addition of free NADH. However, when the enzyme was immobilized simultaneously with a NADH analogue (which also binds to the matrix), a broad endotherm with a Ttr of 91.5 degrees C was obtained, indicating the presence of immobilized enzyme molecules both with, and without, associated NADH. Corresponding increases in heat stability were observed for LDH in solution in the presence of NADH, NAD+, and AMP, leading to increases in Ttr from 72 to 79.5 and 74 and 73 degrees C, respectively. The addition of pyruvate and NAD+ to the enzyme to form an abortive ternary complex led to the same stabilization as that observed with NADH, attendant with a large increase in the enthalpy of transition, deltaHtr. In these studies the technique of DSC was utilized because it is applicable both to soluble and immobilized enzymes and (1) provides rapid information about Ttr and thus thermal stability of enzymes, (2) different energetic states of an enzyme molecule can be identified, and (3) an overall picture of the thermal process is rapidly obtained.
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PMID:Studies on conformation of soluble and immobilized enzymes using differential scanning calorimetry. 1. Thermal stability of nicotinamide adenine dinucleotide dependent dehydrogenases. 19 52

The liver cells of 8 rabbits fed for 12 to 16 weeks with a cholesterol diet showed a decrease of RNA and a stronger reactivity for acid phosphatase and beta-glucuronidase. The non-specific esterase showed a weaker reactivity in the cells with a larger amount of cholesterol and a stronger reaction in the cells with a smaller quantity of this substance. Several enzymes such as: diaphorases, those of the pentose shunt and respiratory cycle as well as those related to the metabolism of lipids, proteins and mucopolysaccharides showed a unconspicuous reactivity. The glycogen was found in a lesser amont in 6 out of 8 rabbits but with a higher concentration in 2 of them. The reactivity of UDPG-GT, active phosphorylase, F-1,6-PA, F-1,6-P Ald, LDH and ADH was stronger in the last 2 animals but weaker in the 6 others. In this 8 rabbit group the total phosphorylase and G-6-PA showed respectively always a stronger and a weaker reactivity than their controls. In the liver of 2 cholesterol-fed for 20 weeks rabbits it was observed a centrolobular fibrosis, a smaller amount of RNA and glycogen as well as a global decrease of the enzymatic reactivity.
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PMID:Histochemical reactions of liver cells in cholesterol-fed rabbits. 40 25

The structure and histochemistry of the palmar and plantar skin were studied in four adult male marmosets (two Callithrix jacchus and two Callithrix penicillata). In this skin there exist well-developed epidermal ridges, to which are attached one or two ducts of sweat glands. A thick stratum corneum can be seen in the epidermis, while a distinct stratum lucidum cannot be isolated from the other layers. The stratum granulosum is constituted by one or three layers of cells containing keratohyalin granules. Melanin granulations are mainly concentrated in the basal cells of the epidermal ridges. Dendritic melanocytes and amelanotic melanocytes containing alkaline phosphatase are found among the epidermal cells. Glycogen, UDPG-GT and phosphorylases are mainly present in the middle and lower Malpighian cells of the epidermal ridges. Alkaline phosphatase, ATPase, alanyl amino-peptidase and leucine aminopeptidase were absent in the epidermal cells. SDH, cytochrome oxidase, MAO and a certain number of NAD-dependent dehydrogenases (LDH, ADH, MDH, alpha-GPDH, beta-OHBDH and GDH) showed a stronger reactivity in the basal cells and Malpighian layer. The NADP-dependent enzymes (G-6-PDH, 6-PGDH, cis-aconistase and ICDH) were more reactive in the upper Malpighian layer and stratum granulosum. The stratum corneum showed some acid phosphatase and nonspecific esterase reactivity. The collagenous fibers intertwined with a small number of very thin elastic ones and a larger amount of reticular fibers run almost parallel to the epidermal ridges in the papillary body. In the reticular dermis some fibers are disposed transversely to the epidermal ridges. Meissner corpuscles reactive to butyrylcholinesterase, acetylcholinesterase, nonspecific esterase and G-6-PA are disposed at regular intervals and frequently at each side of the epidermal ridges. Pacinian corpuscles were found only in the hypodermis. The eccrine sweat glands contain glycogen, UDPG-GT and phosphorylase in their secretory, ductal and myoepithelial cells. The secretory part shows a uniform reactivity for every dehydrogenase because it contains only one type of cells (clear cells). The intraepidermal segment of the ducts shows a stronger reactivity to nonspecific esterase and NADP-dependent dehydrogenases than the epithelial cells around it.
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PMID:The skin of the palms and soles of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 86

Histoenzymologic differences between the parotid, paramandibular and submandibular glands were studied in six Callithrix jacchus (four males and two females) and four Callithrix penicillata (three males and one female). The acinous cells of the paramandibular glands showed a stronger reactivity for the diaphorases (NADH2-TR and NADPH2-TR) and for a certain group of enzymes of the carbohydrate metabolism (F-1-6P Ald, LDH, ADH, G-6-PDH and 6-PGDH), lipid metabolism (alpha-GPDH, beta-OHBDH, alkaline phosphatase and acid phosphatase), protein metabolism (alanyl aminopeptidase, leucine aminopeptidase and GDH) and respiratory chain (cris-aconitase and ICDH). The nonspecific esterase was more reactive in the basal part of of the mucous cells of the submandibular glands. Conversely, some enzymes of the respiratory chain (SDH, cytochrome oxidase and ATPases) showed a stronger reactivity in the serous cells of the parotid and submandibular glands. The paramandibular glands exhibited a lesser autonomic innervation than the parotid and submandibular.
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PMID:Histochemical differences between the major salivary glands of the marmosets (Callithrix jacchus and Callithrix penicillata). 82 38

Sixteen strains of trypanosomes isolated from the blood of 10 freshwater fish species (all but one from South Bohemia) were characterized by enzyme analysis using disc electrophoresis in 5% polyacrylamide gel. Six enzymes were selected: ADH, LDH, MDH, ME, G6PDH and GPI. The most variable were ADH and LDH, whereas MDH, G6PDH and GPI showed the same pattern in all strains analysed. Cluster analysis indicated a very high degree of similarity among strains, even those isolated from phylogenetically distant hosts. Moreover, no correlation between enzyme pattern and host species was found.
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PMID:Enzyme polymorphism of freshwater fish trypanosomes and its use for strain identification. 190 92

Freeze inactivation of LDH, MDH, ADH, G-6-PDH, and PK and its prevention with additives such as sodium glutamate and albumin were studied. LDH, MDH, ADH, G-6-PDH, and PK, each lost their activity during frozen storage at -20 degrees C. The speed of the inactivation differed in each. The stability of the enzymes increased with the increase of the enzyme concentration. Sodium glutamate and albumin prevented the freeze inactivation. While the activity of the LDH solution frozen without additives was almost lost during a day of frozen storage, those frozen with either glutamate (0.2 M) or albumin (0.1%) added decreased less quickly. The residual activity after 1 day was 50% the initial prefreeze value for the former and 10% for the latter, respectively. Combined use of glutamate and albumin prevented the inactivation the best and maintained the initial activity almost completely over 6 weeks. The enzymes tested lost some part of their activity when their solutions were diluted by the media. This inactivation was prevented to a significant extent by the addition of sodium glutamate and/or albumin to the diluting media.
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PMID:Freeze denaturation of enzymes and its prevention with additives. 293 2

The effect of acute treatment of two major Tourette's drugs, haloperidol and pimozide given 60 mg/kg, IP over 48 hr, on hepatic alcohol dehydrogenase (L-ADH) and aldehyde dehydrogenase was studied in the female mouse. The effect of these drugs on heart cytoplasmic lactate dehydrogenase (H-LDH) isoenzyme LDH1 (M) and LDH2 (H) was also measured. Both haloperidol and pimozide significantly inhibited cytoplasmic L-ADH and L-ALDH from controls. Conversely, the haloperidol treatment was associated with induction of both H-LDH isoenzymes studied. Injection of pimozide, 25 mg/kg, IP, to rats with preference to ethanol drinking, caused aversion to voluntary intake of 5% ethanol consumption. This suggests that pimozide produced inhibition of L-ADH in another species and thereby causing aversion to ethanol drinking or may be related to dopaminergic antagonist property. This inhibition of these drugs on the oxidative and reductive pathways of biogenic amine aldehydes may be implicated in and/or associated with the underlying mechanism(s) of action.
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PMID:Tourette's medications: effect on minor oxidative and reductive pathways of biogenic amines. 322 45


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