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:1.1.1.1 (alcohol dehydrogenase)
9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intact pp60c-src, the cellular homologue of the transforming protein of Rous sarcoma virus, was purified from human platelets. The purified fractions also contained small amounts of a 54-kDa proteolytic degradation product of pp60c-src. We investigated some of the biochemical and kinetic properties of pp60c-src protein tyrosine kinase. Maximum kinase activity occurred at pH 6.5 and required a mixture of 2 mM Mn2+/Mg2+ as divalent cations. The enzyme most strongly phosphorylated casein, followed by enolase and alcohol dehydrogenase. The Km value for ATP was 4 microM for substrate phosphorylation and for autophosphorylation. Using casein, we determined a Vmax for substrate phosphorylation by pp60c-src in the range of 1.9-3.4 nmol.min-1.mg-1. Since the Vmax value for the purified 54-kDa fragment of pp60c-src was also included in this value, we conclude that proteolytic degradation of a 6-kDa fragment from the N-terminus of pp60c-src did not affect its kinase activity. Tryptic phosphopeptide analysis identified Tyr-416 as the major autophosphorylation site. Preincubation of purified pp60c-src with ATP increased the amount of autophosphorylation accompanied by an increase in Vmax, whereas the Km values were not altered. Our data directly demonstrate that autophosphorylation at Tyr-416 exerts, in contrast to phosphorylation at Tyr-527, a positive regulatory effect on the pp60c-src kinase activity.
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PMID:Characterization of purified pp60c-src protein tyrosine kinase from human platelets. 169 62

High protein diet is known to increase glomerular filtration rate (GFR) and induce kidney hypertrophy. The mechanisms underlying these changes are not understood. Since the mammalian kidney comprises different nephron segments located in well-delineated zones, it is conceivable that the hypertrophy does not affect all kidney zones and all nephron segments uniformly. The present experiments were designed to study the chronic effects of high or low isocaloric protein diets (HP = 32% or LP = 10% casein, respectively) on kidney function and morphology in Sprague-Dawley rats. HP diet induced significant increases in kidney mass, GFR, free water clearance, and maximum urine concentrating ability. Kidney hypertrophy was characterized by: 1. a preferential increase in thickness of the inner stripe of the outer medulla (IS) (+54%, P less than 0.001, while total kidney height, from cortex to papillary tip, increased only by 18%); 2. a marked hypertrophy of the thick ascending limbs (TAL) in the inner stripe (+40% epithelium volume/unit tubular length, P less than 0.05) but not in the outer stripe nor in the cortex; 3. an increase in heterogeneity of glomeruli between superficial (S) and deep (D) nephrons (D/S = 1.47 in HP vs. 1.17 in LP, P less than 0.05). In contrast, normal kidney growth with age and kidney hypertrophy induced by uninephrectomy were not accompanied by preferential enlargement of IS structures. The morphologic changes induced by high protein intake parallel those we previously reported in rats fed a normal diet (25% protein) but in which the operation of the urine concentrating mechanism was chronically stimulated by ADH infusion or by reduction in water intake.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Role of the urinary concentrating process in the renal effects of high protein intake. 317 35

The mechanisms by which high protein intake increases filtration rate and kidney hypertrophy in health and may be detrimental to the kidney in chronic renal failure are not well understood. We studied the kidneys of Sprague Dawley rats fed high (HP) and low (LP) isocaloric protein diets (32% and 10% casein, respectively) for 4 weeks. HP induced significant increases in kidney mass, GFR, and maximum urine concentrating ability (UMax). Kidney hypertrophy was characterized by (1) a selective increase in thickness of the inner stripe of the outer medulla (IS, +54%, P less than 0.001) while total kidney height (from cortex to papillary tip) increased only by 18%; (2) a considerable hypertrophy of the thick ascending limbs (TAL) in the IS (+43% epithelium volume/unit tubular length) but not in the outer stripe nor in the cortex; and (3), an increase in heterogeneity of glomerular volume between superficial and deep nephrons (P less than 0.05). these morphologic changes parallel those we previously reported in rats fed a normal protein diet (25% casein) but in which the operation of the urine concentrating mechanism was chronically stimulated by ADH infusion or by reduction in water intake. In contrast, normal kidney growth with age or kidney hypertrophy induced by uninephrectomy were not accompanied by preferential enlargement of IS structures.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Possible role of the thick ascending limb and of the urine concentrating mechanism in the protein-induced increase in GFR and kidney mass. 348 Sep 97

Commercially available crystalline yeast alcohol dehydrogenase contained protein kinase activity. Casein and phosvitin were readily phosphorylated, but whole calf thymus histone was not. The protein kinase activity was inhibited by KCl, was not stimulated by cyclic AMP and could be separated from the alcohol dehydrogenase activity by sucrose density centrifugation.
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PMID:Protein kinase activity in commercially available crystalline yeast alcohol dehydrogenase. 435 9

The effects of two liquid diets, Sustacal and Shorey-AIN, on liver alcohol dehydrogenase (ADH) activity and ethanol clearance were tested in rats under conditions of high ethanol exposure for nine days. High blood ethanol levels (BEL) were produced through a combination of an initial intubated dose of ethanol sustained ethanol release tube (SERT), and ethanol as 37% of total energy in the liquid diet. Under free-feeding conditions, rats consumed slightly more ethanol per unit body weight in the Shorey-AIN diet, a diet formulated for rodent nutrition, than in the Sustacal diet, a diet originally intended for human consumption. However, BEL were significantly higher in the Sustacal group than in the Shorey-AIN group. No differences in ethanol clearance rates were observed between the groups. On the other hand, total liver ADH activity was significantly reduced in both the Shorey AIN/ethanol and the Sustacal/ethanol groups, compared to lab chow controls. When the Sustacal diet was fortified with casein and methionine so that the protein content matched that of the Shorey AIN diet, the BEL were no longer significantly higher than those produced by the Shorey AIN/ethanol diet. The results demonstrate the effect of nutritional factors on BEL under conditions of high ethanol load. However, these factors do not appear to alter major characteristics of ethanol metabolism and clearance in our short-term experiments.
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PMID:Effects of different liquid diets and sustained ethanol release on alcohol metabolism. 639 9

alpha-Crystallin, a major protein component of the lens, has chaperone-like properties whereby it prevents destabilised proteins from precipitating out of solution. It does so by forming a soluble high-molecular-weight (HMW) complex. A spectroscopic investigation of the HMW complex formed between a variety of unfolded proteins and bovine alpha-crystallin is presented in this paper. As monitored by fluorescence spectroscopy, a large amount of the hydrophobic probe, 8-anilino-1-naphthalene sulfonate (ANS) binds to the HMW complex implying that the complexed proteins (alcohol dehydrogenase (ADH), gamma-crystallin and rhodanese) are bound in an unfolded, possibly molten-globule state. The interaction between the anionic surfactant, sodium dodecyl sulfate (SDS) and ADH at high temperatures gives rise to a similar large increase in ANS fluorescence to that for the complex between alpha-crystallin and ADH. SDS, like alpha-crystallin, therefore complexes to proteins in their unfolded state leaving a large hydrophobic surface exposed to solvent. Unlike other chaperones (e.g., GroEL, DnaK and SecB), alpha-crystallin does not interact with unfolded, hydrophobic but stable proteins (e.g., reduced and carboxymethylated alpha-lactalbumin and alpha-casein). It is concluded that alpha-crystallin will only complex with proteins that are about to precipitate out of solution, i.e., ones that are severely compromised. 1H-NMR spectroscopy of the HMW complex formed between alpha-crystallin and gamma-crystallin indicates that the short C-terminal extension of alpha B-crystallin, but not that of alpha A-crystallin, has lost its flexibility in the complex implying that the former is involved in interactions with the unfolded gamma-crystallin molecule, possibly electrostatically via its two C-terminal lysine residues.
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PMID:On the interaction of alpha-crystallin with unfolded proteins. 757 31

The objective of this study was to determine the effect of a lysine-deficient diet on carnitine status in adult rats and subsequently on ethanol metabolism. Adult male rats were fed either the AIN-76 diet (NS), the AIN-76 diet with wheat gluten (WG) replacing casein, the WG diet plus 0.8% L-lysine (LS), or the LS diet plus 0.5% L-carnitine (CS) for 30 days. On the 31st day the rats were given an oral dose of ethanol and blood-ethanol concentrations (BEC) were monitored for the next 8 hours. One week later the rats were given a second dose of ethanol and urine was collected until killed, 3 hours post-ethanol administration (PEA). Besides growth retardation and hypoproteinemia, BEC were significantly elevated in the WG group compared to the other group at hours 3-8 PEA. There were no significant differences in BEC between the LS and CS groups; however, their BEC were significantly higher than that of the NS group. The BEC were inversely related to liver alcohol dehydrogenase (ADH) activities which were significantly lower in WG, LS and CS groups than in the NS group. Plasma, liver and urine carnitine values were significantly higher in the CS group than in the NS, WG and LS groups, wherein the values were similar. It is concluded that the WG diet reduced ADH activity and attenuated ethanol metabolism without significantly altering blood, liver and urinary carnitines in the adult rat.
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PMID:Wheat gluten-based diet retarded ethanol metabolism by altering alcohol dehydrogenase and not carnitine status in adult rats. 846 15

Untagged recombinant human small heat shock protein with apparent molecular mass 22 kDa (Hsp22) was obtained in homogeneous state. Size exclusion chromatography and chemical crosslinking with dimethylsuberimidate indicate that Hsp22 forms stable dimers. Being highly susceptible to oxidation Hsp22 forms disulfide crosslinked dimers and poorly soluble high molecular mass oligomers. According to CD spectroscopy oxidation of Hsp22 results in disturbing of both secondary and tertiary structure. Hsp22 possesses a negligibly low autophosphorylation activity and under the conditions used is unable to phosphorylate casein or histone. Hsp22 effectively prevents heat-induced aggregation of yeast alcohol dehydrogenase and bovine liver rhodanese with chaperone activity comparable to that of recombinant human small heat shock protein with apparent molecular mass 20 kDa (Hsp20).
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PMID:Some properties of human small heat shock protein Hsp22 (H11 or HspB8). 1535 70

The caseins are major components of milk for most mammals and are secreted as large colloidal aggregates termed micelles. They have less ordered secondary and tertiary structures in comparison with typical globular proteins. In this work, beta-casein, a member of the casein family, has been demonstrated to exhibit chaperone-like activity, being able to suppress the thermal and chemical aggregation of such substrate proteins as insulin, lysozyme, alcohol dehydrogenase, and catalase by forming stable complexes with the denaturing substrate proteins. Meanwhile, beta-casein was found to not only prevent aggregation of the substrate proteins, but also solubilize the protein aggregates already formed. Data also show that beta-casein exhibits a higher chaperone-like activity than alpha-casein, likely due to the difference in the number of proline residues present and/or in the extent of exposed hydrophobic surfaces. The implications for their in vivo functions of the caseins, based on their exhibiting such in vitro chaperone-like activities, are discussed.
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PMID:Chaperone-like activity of beta-casein. 1577 87

The fate of DNA and protein transgenic sequences in products derived from animals fed transgenic crops has recently raised public interest. Sensitive molecular tests targeting the Bt176 genetic construct and the transgenic Cry1Ab protein were developed to determine whether plant sequences, especially transgenic sequences, are present in animal products. A protocol for total DNA extraction and purification from cow whole blood samples was first drawn up and assessed by spiking with known amounts of DNA from Bt176 maize. The limit of detection for transgenic sequences (35S promoter and Bt176-specific junction sequence) was determined by both the polymerase chain reaction-enzyme-linked immunosorbent assay (PCR-ELISA) and the 5'-nuclease PCR assay. Four additional PCR systems were built to substantiate the results. The first detects a mono-copy maize-specific sequence (ADH promoter). Two others target multi-copy sequences from plant nucleus (26S rRNA gene) and chloroplast (psaB gene). The last one, used as a positive control, targets a mono-copy animal sequence (alpha(s1)-casein gene). Both methods detected a minimum spiking at 25 copies of Bt176 maize/mL in 10 mL whole blood samples. The sandwich ELISA kit used detected down to 1 ng transgenic Cry1Ab protein/mL spiked whole blood.
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PMID:Detection of genetically modified corn (Bt176) in spiked cow blood samples by polymerase chain reaction and immunoassay methods. 1586 34


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