Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The outer tegument membranes of Schistosoma mansoni schistosomula have been removed by mechanical disruption in a hypotonic salt solution and partially purified by differential and sucrose density gradient centrifugation. Fractionation was monitored by measuring increase in specific activity of bound [125I]wheat-germ agglutinin (WGA), alkaline phosphatase and calcium-stimulated ATPase. Two-dimensional IEF/SDS polyacrylamide gel electrophoresis was used to analyse the peptide composition of the isolated membranes and to compare and contrast with lactoperoxidase/glucose oxidase surface labelled peptides. At least 35 surface-labelled peptides were resolved on the two-dimensional maps: all were also present in the membrane material recovered from the sucrose gradient. Western blot analysis demonstrated a marked heterogeneity in the antibody response of infected human patients to individual membrane antigens. The antigenic profile of membranes isolated from cercariae, 18 and 96 h schistosomula were compared using Western blots: some minor differences were observed between the three preparations.
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PMID:Isolation and antigen analysis of surface tegument membranes from schistosomula of Schistosoma mansoni. 624 13

Vitamin D3 is known to stimulate the absorption of calcium across the asymmetric intestinal epithelial cells. Efforts to elucidate the mechanism of stimulation of intestinal calcium transport by vitamin D are now focused on evaluating the protein composition and topology of the brush-border membrane and its associated core material. Intestinal brush-border membranes were isolated from vitamin D-replete and vitamin D-deficient chicks. Core material proteins were isolated, by sedimentation, from brush-border membranes which were solubilized with Triton X-100. As determined by polyacrylamide gel electrophoresis, dietary vitamin D3 treatment caused no change in the relative amounts of five major core material proteins with Mr = 101,000, 94,000, 67,000, 42,000 (actin), and 17,000. In contrast, dietary vitamin D3 treatment caused a significant reduction in the levels of two proteins with Mr = 111,000 (sucrase) and 83,000, and an increase in the levels of a protein with Mr = 78,000 (possibly a subunit of alkaline phosphatase). The Mr = 111,000, 83,000, and 78,000 proteins are readily solubilized by Triton X-100 and are located on the extracellular surface of the brush-border membrane, as judged by [125I]diazoiodosulfanilic acid and lactoperoxidase 125I labeling. A significant vitamin D-dependent difference was found with respect to iodination of isolated core material as evidenced by the 125I labeling patterns of the Mr = 42,000 protein (actin). The Mr = 42,000 protein was labeled two to three times more extensively when associated with core material derived from vitamin D-deficient chicks as compared to vitamin D-replete chicks. Increasing the salt concentration (0-125 mM KCl) present during core material isolation from either vitamin D-replete or vitamin D-deficient chicks yields core material actin which is more susceptible to iodination by both [125I]diazoiodosulfanilic acid and lactoperoxidase. This increase in the extent of actin iodination is coupled to a salt-induced decrease in the stability of the core material which is evidenced by a decrease in the percentage of total brush-border membrane actin which is Triton-insoluble. This strongly suggests that the vitamin D-induced decrease in the accessibility of actin to iodination reagents results from a vitamin D-dependent change in the structure of the core material. Collectively, these results implicate a role for dietary vitamin D3 in maintaining a specified composition and topology of both the brush-border membrane proteins as well as its associated cytoskeletal core proteins, which is possibly important for intestinal calcium transport.
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PMID:Vitamin D. Its effect on the protein composition and core material structure of the chick intestinal brush-border membrane. 630 7

The effects of sodium butyrate, dimethyl sulfoxide (DMSO), and retinoic acid on the growth, morphology, carcinoembryonic antigen content, cell surface membrane-associated enzyme activities, and glycoprotein profiles of a human rectal adenocarcinoma cell line (HRT-18) in culture were compared. All three agents reversibly caused a marked increase in doubling times, a decrease in saturation densities, and a markedly reduced colony-forming efficiency in soft agar. Only butyrate caused gross morphological changes including cell enlargement, flattening, and increased membranous process formation. Carcinoembryonic antigen content was increased during culture in butyrate, while it was reduced by DMSO and unchanged by retinoic acid. The activities of membrane-associated enzymes were altered significantly in the butyrate-treated cells. For example, an increase in the activities of alkaline phosphatase (10-fold), gamma-glutamyl transpeptidase activity (3-fold) and sucrase activity (2-fold) was observed, while those of aminooligopeptidase and K+-stimulated phosphatase actually showed slight decreases. DMSO- or retinoic acid-treated cells showed a marked decrease in alkaline phosphatase activity, but other enzyme activities remained unchanged. Surface protein-labeling patterns of lactoperoxidase-catalyzed iodinated HRT-18 cells showed no significant change from the control cells following treatment with DMSO or retinoic acid. The most prominent change caused by butyrate treatment was the appearance of a major glycoprotein band with an apparent molecular weight of 60,000. These data indicate that the use of butyrate, DMSO, and retinoic acid may provide useful information concerning the identification of differentiation-associated markers of human rectal cancer cells. Furthermore, these agents, although having similar effects on the growth properties, have different effects on the morphology and on the biochemical properties of human rectal cancer cells.
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PMID:Differential effects of sodium butyrate, dimethyl sulfoxide, and retinoic acid on membrane-associated antigen, enzymes, and glycoproteins of human rectal adenocarcinoma cells. 705 70

Previous histochemical and biochemical localizations of alkaline phosphatase in Bacillus licheniformis MC14 have shown that the membrane-associated form of the enzyme is located on the inner surface of the cytoplasmic membrane, and soluble forms are located in the periplasmic space and in the growth medium. The distribution of salt-extractable alkaline phosphatase on the surfaces of the cytoplasmic membrane of B. licheniformis MC14 was determined by using lactoperoxidase-125I labeling techniques. Cells harvested during rapid alkaline phosphatase production were converted to protoplasts or lysed protoplasts and labeled. Analysis of the data obtained indicated that 30% of the salt-extractable, membrane-associated alkaline phosphatase was located on the outer surface of the cytoplasmic membrane, whereas 70% of the membrane-associated enzyme was localized on the inner surface. Controls for protoplast integrity (release of tritiated thymidine or examination of cytoplasmic proteins for label content) indicated excellent protoplast stability. Controls indicated that chemical labeling was not a factor in the apparent distribution of alkaline phosphatase on the membrane. These results support the previously reported histochemical localization of alkaline phosphatase on the membrane inner surface. The presence of alkaline phosphatase on the membrane outer surface is reasonable, considering the soluble forms of the enzyme found in the periplasmic region and in the culture medium.
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PMID:Lactoperoxidase-125I localization of salt-extractable alkaline phosphatase on the cytoplasmic membrane of Bacillus licheniformis. 746 64

The effect of continuous flow high-intensity ultrasound (with and without heat generation) on alkaline phosphatase, gamma-glutamyltranspeptidase, lactoperoxidase, whey proteins (alpha-lactalbumin and beta-lactoglobulin), casein, and fat was studied in milk. Results were compared with those obtained using a conventional heating system having similar processing conditions. Hardly any effect on enzymes was observed when ultrasound was applied without heat generation. The highest denaturation of enzyme and whey proteins was found in samples subjected to ultrasound and heat. At 61, 70, and 75.5 degrees C a synergistic effect between ultrasound and heat was observed for the inactivation of alkaline phosphatase, gamma-glutamyltranspeptidase, and lactoperoxidase, respectively. A noticeable synergism between ultrasound and heat was detected for alpha-lactalbumin and beta-lactoglobulin denaturation. No changes in the casein were observed after any of the conditions assayed. As a consequence of ultrasound effects, a substantial reduction (up to 81.5%) in the size of the fat globule was observed. When 70 and 75.5 degrees C were achieved during high-intensity ultrasonic homogenization, a better particle distribution was observed as compared to that obtained at lower temperatures. This work describes the influence of continuous flow high-intensity ultrasound on important milk components as a first step for future processing applications.
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PMID:Influence of high-intensity ultrasound and heat treatment in continuous flow on fat, proteins, and native enzymes of milk. 1069 59

A detailed kinetic study of alkaline phosphatase, lactoperoxidase and beta-lactoglobulin was carried out in the context of identifying intrinsic time-temperature indicators for controlling the heat processing of milk. The heat inactivation or denaturation of alkaline phosphatase, lactoperoxidase and beta-lactoglobulin under isothermal conditions was found to follow first order kinetics. Experimental results were analysed using both a two step linear regression and a one step non-linear regression method. Results obtained using the two statistical techniques were comparable, but the 95% confidence interval for the predicted values was smaller when the one step non-linear regression method was used, indicating its superiority for estimating kinetic parameters. Thermal inactivation of alkaline phosphatase and lactoperoxidase was characterized by z values of 5.3 deg C (D60 degrees C = 24.6 min) and 4.3 deg C (D71 degrees C = 38.6 min) respectively. For the denaturation of beta-lactoglobulin we found z values of 7.9 deg C (D7.5 degrees C = 49.9 min) in the temperature range 70-80 degrees C and 24.2 deg C (D85 degrees C = 3.53 min) in the range 83-95 degrees C. Dref and z were evaluated under dynamic temperature conditions. To estimate the statistical accuracy of the parameters, 90% joint confidence regions were constructed.
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PMID:Inactivation kinetics of alkaline phosphatase and lactoperoxidase, and denaturation kinetics of beta-lactoglobulin in raw milk under isothermal and dynamic temperature conditions. 1128 74

In the context of identifying intrinsic time temperature integrators (TTIs) for evaluating heat processing of milk, the extent to which milk fat content has an effect on alkaline phosphatase (ALP) and lactoperoxidase (Lpo) inactivation and on beta-lactoglobulin (beta-Ig) denaturation kinetics was studied. Inactivation and denaturation kinetics were analysed in whole, semi-skimmed and skimmed milk. In previous experiments (isothermal and non-isothermal heating conditions), heat inactivation of ALP and Lpo and heat denaturation of beta-Ig were found to follow first order kinetics. This allowed experimental design to be simplified. Data analysis was performed by non-linear regression and results were evaluated by construction of joint confidence regions. The possible effect of milk fat was illustrated by temperature time tolerance (TTT-) diagrams. Although initial ALP activity was lower in skimmed milk compared with semi-skimmed or whole milk, kinetics were comparable and fat content did not seem to substantially affect the ALP test result for pasteurized milk. Unlike ALP, Lpo inactivation and beta-Ig denaturation kinetics differed significantly in milk with different fat content. Differences between Lpo inactivation kinetics were relatively small and acceptable in the context of quantifying the process impact. Denaturation of beta-Ig, on the other hand, seemed to be enhanced at higher milk fat content (> 72 degrees C).
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PMID:Kinetics of alkaline phosphatase and lactoperoxidase inactivation, and of beta-lactoglobulin denaturation in milk with different fat content. 1246 92

Six milk compounds were studied as potential intrinsic time temperature integrators (TTIs) for the assessment of heat-treated milk. These include the enzymes alkaline phosphatase and lactoperoxidase, the whey protein beta-lactoglobulin and the chemical compounds hydroxymethylfurfural, lactulose and furosine. In previous research the inactivation/denaturation/formation kinetics of these compounds were analyzed under isothermal and nonisothermal conditions and evaluated for variability of the milk composition. The present paper focuses on the implementation of the TTIs. TTIs are validated with respect to microbiological indices and quality attributes, and a quantitative relationship between the denaturation, inactivation or formation of the TTIs and technological processes is established by construction of general time temperature tolerance (TTT) diagrams. In these diagrams temperature time combinations are presented, which lead to the same formation, inactivation or denaturation of TTIs, or result in the same level of microbiological destruction or quality degradation of the product. TTT-diagrams are very informative since they allow visualization of the impact of a thermal process on milk and evaluation of criteria for evaluating milk authenticity (conformity of the product with the terminology applied). Moreover, the optimum combination of temperature and time of heating may be readily deduced from these diagrams.
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PMID:From time temperature integrator kinetics to time temperature integrator tolerance levels: heat-treated milk. 1476 17

Studies of the potential of high pressure homogenisation (HPH) for the combined pasteurisation/ homogenisation of raw bovine milk were undertaken. Raw milk was preheated to 45 degrees C and HPH-treated at 150, 200 or 250 MPa; milk outlet temperature at these pressures were 67, 76.8 and 83.6 degrees C, respectively, with a holding time of approximately 20 s. Raw and commercially pasteurized and homogenized (CPH) milk samples were analysed as controls. Fat globules in HPH samples were approximately half the size of those in CPH samples, although differences were not significant (P>0.05). beta-Lactoglobulin was denatured at pressures > or =150MPa, although little denaturation of alpha-lactalbumin was observed. Numbers of psychrotrophic bacteria in raw milk were reduced by 2.73 log cycles by HPH at 150 MPa and were uncountable following HPH at 200 or 250 MPa. Mesophilic bacterial counts were reduced by 1.30, 1.83 and 3.06 log cycles by HPH at 150, 200 or 250 MPa, respectively. No viable Staphylococcus aureus nor coliform cells remained in any HPH milk samples. HPH did not affect the colour of milk and HPH samples did not cream during refrigerated storage. The activities of plasmin, alkaline phosphatase and lactoperoxidase in milk were all greatly reduced by HPH. Pseudomonas fluorescens, inoculated into milk (approximately 10(6) cfu/ml), was reduced to undetectable levels by HPH at 200MPa (milk inlet temperature, approximately 10 degrees C); however, Ps. fluorescens proteinase was quite resistant to HPH under such conditions. Overall, owing to the significant increase in temperature and the possibility of varying the holding time, there may be potential applications for HPH as a novel liquid milk processing technique, combining many advantages of conventional homogenization and pasteurization of milk in a single process.
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PMID:Potential applications of high pressure homogenisation in processing of liquid milk. 1574 28

High pressure homogenisation (HPH) is a novel dairy processing tool, which has many effects on enzymes, microbes, fat globules and proteins in milk. The effects of HPH on milk are due to a combination of shear forces and frictional heating of the milk during processing; the relative importance of these different factors is unclear, and was the focus of this study. The effect of milk inlet temperature (in the range 10-50 degrees C) on residual plasmin, alkaline phosphatase, lactoperoxidase and lipase activities in raw whole bovine milk homogenised at 200 MPa was investigated. HPH caused significant heating of the milk; outlet temperature increased in a linear fashion (0.5887 degrees C/ degrees C, R2=0.9994) with increasing inlet temperature. As milk was held for 20 s at the final temperature before cooling, samples of the same milk were heated isothermally in glass capillary tubes for the same time/temperature combinations. Inactivation profiles of alkaline phosphatase in milk were similar for isothermal heating or HPH, indicating that loss of enzyme activity was due to heating alone. Loss of plasmin and lactoperoxidase activity in HPH milk, however, was greater than that in heated milk. Large differences in residual lipase activities in milks subjected to heating or HPH were observed due to the significant increase in lipase activity in homogenised milk. Denaturation of beta-lactoglobulin was more extensive following HPH than the equivalent heat treatment. Inactivation of plasmin was correlated with increasing fat/serum interfacial area but was not correlated with denaturation of beta-lactoglobulin. Thus, while some effects of HPH on milk are due to thermal effects alone, many are induced by the combination of forces and heating to which the milk is exposed during HPH.
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PMID:Significance of frictional heating for effects of high pressure homogenisation on milk. 1622 53


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