SEARCH · Search PubMed

Results for “LACTOSE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,387 records · Page 77Linked to original sources

PubMed1985

Purification of anti-lactose antibodies from antisera to Neisseria gonorrhoeae and Neisseria meningitidis.

Lactosyl-sepharose 4B columns were used for purification by affinity chromatography of anti-lactose antibodies from rabbit antisera to the gonococcal strains 8551 and VII, and the serogroup B meningococcal strain M982. Anti-lactose antibodies were obtained from all three antisera. SDS-PAGE of lipopolysaccharide and of bacterial cells and immunoblotting with the anti-lactose antibodies showed that the lipopolysaccharide was the only bacterial component with binding sites for the antibodies.

Animals↗

PubMed1998

Lactose intolerance and irritable bowel syndrome.

A recent study on lactose intolerance and irritable bowel syndrome has shown that subjective lactose intolerance is increased in patients with irritable bowel syndrome, despite no increase in the prevalence of lactose maldigestion.

Adult↗

PubMed1994

Study of the compaction mechanisms of lactose-based direct compression excipients using indentation hardness and Heckel plots.

Indentation hardness of tablet surfaces has been used to determine the consolidation mechanisms of the lactose-based excipients Fast Flo Lactose, Ludipress, Cellactose and Tablettose. The Leuenberger equation has been modified to obtain values of compressibility and compactability by using a value of compactability obtained from a tablet at maximum applied force and by substituting deformation resistance by relative deformation resistance. Also, parameters obtained from plots of the Heckel tablet-indie and ejected-tablet methods were calculated in order to establish the comparative consolidation mechanisms in the lactose-based excipients under study. The possibility of using the absolute value of the difference between upper and lower surface hardnesses of the tablets made on an eccentric press is suggested as an alternative method to determine the comparative consolidation mechanisms of different substances.

Cellulose↗

PubMed1990

The effect of continued feeding of physiological amounts of lactose on the level of intestinal lactase and other disaccharidase enzyme activities in the rat.

Intestinal lactase activity in mammals is high at birth but begins to decline around weaning and reaches very low levels in adult life. The triggering mechanism for this decline is not clear. Because of the association of the decline with weaning, lack of lactose in the diet has been implicated. In 110 growing rats, the effect of continued supplementation of the diet after weaning with physiological amounts of either cows' milk or a 5% lactose solution on intestinal lactase and other disaccharidase enzyme activities was investigated. In both control and test animals, the specific lactase activity decreased from a peak value of 115 +/- 4 mumol min-1 g-1 protein before weaning to about 10% at maturity. There was no significant difference in the level or the pattern of decline between the groups. Sucrase, maltase and trehalase showed the normal maturational changes without being affected by the test diets. The finding suggests that diet, particularly the presence or absence of physiological amounts of lactose, has no appreciable effect on the age related spontaneous decline of intestinal lactase activity or on the pattern of development of the other disaccharidases.

Aging↗

PubMed1969

Lactose synthetase: progesterone inhibition of the induction of alpha-lactalbumin.

Lactose synthesis in the mammary gland is dependent on the hormonally controlled synthesis of the two protein components of lactose synthetase, alpha-lactalbumin and a galactosyltransferase. Prolactin induces the synthesis of both proteins in mammary gland explants treated with insulin and hydrocortisone, but the induction kinetics cannot account for the asynchronous synthesis of the two proteins that are observed in vivo. Progesterone appears to take part in the control of lactose synthesis and acts to repress the formation of alpha-lactalbumin throughout pregnancy. At parturition, when the concentration of progesterone in the plasma decreases, the rate of alpha-lactalbumin synthesis increases.

Albumins↗

PubMed1981

Lactose facilitates the intestinal absorption of lead in weanling rats.

The milk sugar lactose is known to facilitate calcium absorption and has been shown to enhance the uptake of essential trace metals from the intestines as well. Its physiological role as the major carbohydrate source for suckling mammals is thus complemented by its ability to facilitate the absorption of necessary minerals. The studies reported here show that the intestinal absorption of lead and its uptake into blood, liver, kidney, and bone are also increased by lactose in young weanling rats. These data extend the known range of lactose facilitation of mineral absorption to a nonessential, toxic element, confirming the nonspecificity of its action on the gut. In addition, they suggest an explanation for some of the conflicting evidence regarding the prophylactic efficacy of milk in lead poisoning.

Age Factors↗

PubMed1976

Plasmids in Streptococcus lactis: evidence that lactose metabolism and proteinase activity are plasmid linked.

Populations of lactose positive (Lac+) and proteinase positive (Prt+) cells from Streptococcus lactis M18, C10, and ML3 grown at 39 degrees C gave rise to increasing proportions of Lac- Prt- clones. The deficiencies did not appear until after a number of generations at the elevated temperature, and the rate depended on the strain.Lac- Prt+ and Lac+ Prt- mutants were isolated after treatment with ethidium bromide. Plasmid deoxyribonucleic acid was isolated by cesium chloride-ethidium bromide equilibrium density gradient centrifugation from the parent cultures as well as from their Lac- Prt-, Lac- Prt+, and Lac+ Prt- mutants. Five distinct plasmid sizes of approximate molecular weights of 2,4, 8, 21, and 27 million were found in S. lactis C10, whereas the Lac- Prt- derivative lacked the 8- and 21-million-dalton plasmids, but the 8-million-dalton plasmid was present in the Lac-Att mutant. In S. lactis m18 five plasmids possessing molecular weights of about 2, 4, 10, 18 and 27 million were observed. The 10- and 18-million-dalton plasmids were not detected in the Lac- Prt- mutants, whereas the Lac- Prt+ derivative lacked only the 18-million-dalton plasmid and the Lac+ Prt- mutant lacked only the 10-million-dalton plasmid. In S. lactis ML3 five distinct plasmids, with approximate molecular weights of 2, 4, 8, 22, and 30 million, were present. The 8- and 22-million-dalton plasmids were not detected in the Lac- Prt- derivative, but the 8-million-dalton plasmid was present in the Lac- Prt+ mutant. The evidence suggests that lactose-fermenting ability and proteinase activity in these organisms are mediated through two distinct plasmids having molecular weights of 8 x 10(6) to 10 x 10(6) for proteinase activity and 18 x 10(6) to 22 x 10(6) for lactose metabolism.

DNA, Bacterial↗

PubMed1984

Regulation of product formation during glucose or lactose limitation in nongrowing cells of Streptococcus lactis.

Nongrowing cells of Streptococcus lactis in a pH-stat were dosed with sugar to allow fermentation at the maximum rate or were fed a continuous supply of sugar at rates less than the maximum. Under anaerobic conditions, rapid fermentation of either glucose or lactose was essentially homolactic. However, with strain ML3, limiting the fermentation rate diverted approximately half of the pyruvate to formate, acetate, and ethanol. At limiting glucose fermentation rates, cells contained lower concentrations of lactate dehydrogenase activator (fructose 1,6-diphosphate) and pyruvate formate-lyase inhibitors (triose phosphates). As a result, pyruvate formate-lyase and pyruvate dehydrogenase play a greater role in pyruvate metabolism. In contrast to strain ML3, strain ML8 did not give the same diversion of products under anaerobic conditions, and cells retained higher concentrations of the above effector compounds. Lactose metabolism under aerobic conditions resulted in pyruvate excretion by both S. lactis ML3 and ML8. At 7% of the maximum utilization rate, pyruvate accounted for 69 and 35% of the lactose metabolized by ML3 and ML8, respectively. Acetate was also a major product, especially with ML8. The data suggest that NADH oxidase is involved in coenzyme recycling in the presence of oxygen and that pyruvate formate-lyase is inactivated, but the pyruvate dehydrogenase complex still functions.

Aerobiosis↗

PubMed1990

Construction of lactose-utilizing Xanthomonas campestris and production of xanthan gum from whey.

Xanthomonas campestris pv. campestris possesses a low level of beta-galactosidase and therefore is not able to grow and produce significant amounts of xanthan gum in a medium containing lactose as the sole carbon source. In this study, a beta-galactosidase expression plasmid was constructed by ligating an X. campestris phage phi LO promoter with pKM005, a ColE1 replicon containing Escherichia coli lacZY genes and the lpp ribosome-binding site. It was then inserted into an IncP1 broad-host-range plasmid, pLT, and subsequently transferred by conjugation to X. campestris 17, where it was stably maintained. The lacZ gene under the control of the phage promoter was expressed at a high level, enabling the cells to grow in a medium containing lactose. Production of xanthan gum in lactose or diluted whey by the engineered strain was evaluated, and it was found to produce as much xanthan gum in these substrates as the cells did in a medium containing glucose.

Cloning, Molecular↗

PubMed1969

Neisseria lactamicus sp. n., a lactose-fermenting species resembling Neisseria meningitidis.

The biochemical and serological characteristics of lactose-utilizing strains of Neisseria were determined. These organisms were found in the nasopharynx of man and grew well on Thayer-Martin Selective Medium. They were compared with N. meningitidis to ascertain whether they were variants of this species. Differences between the lactose-using strains and the recognized species of Neisseria were considered significant enough to warrant designation of a new species, Neisseria lactamicus. This group has not been widely recognized as being separate from N. meningitidis; therefore, the normal incidence and clinical significance of these organisms has not been fully established. These organisms are oxidase-positive and positive for beta-D-galactosidase activity; they demonstrate fermentation in King Oxidation-Fermentation Medium; and they produce acid from only glucose, lactose, and maltose, of the 27 substrates incorporated in Cystine Trypticase Agar. Individual strains vary in their ability to grow on Nutrient Agar at both 25 and 37 C and in their pigmentation on Loeffler Medium. Results indicated that these organisms are serologically distinct from the N. meningitidis serogroups. Only 34 of 116 strains of N. lactamicus were smooth and could be tested by slide agglutination. None of the 34 could be grouped as N. meningitidis group A, B, C, D, X, Y, or Z. Thirty-one of these strains could, however, be specifically grouped with antisera prepared with N. lactamicus strains. Cross absorptions confirmed that N. lactamicus is serologically distinguishable from N. meningitidis.

Culture Media↗

PubMed1973

Lactose-fermenting Salmonella from dried milk and milk-drying plants.

A study of 552 salmonella cultures revealed that 86 (15.6%) of the cultures fermented lactose. These had been isolated from dried milk products and milk-drying plants. Acid and gas were produced in lactose broth. Solid media containing lactose as the key ingredient for the differential reaction were not satisfactory for recognizing salmonella colonies. No problem was encountered in selecting salmonella colonies when bismuth sulfite agar was used.

Animals↗

PubMed1983

Prevalence of viridans streptococci exhibiting lactose-inhibitable coaggregation with oral actinomycetes.

Fresh oral isolates from human dental plaque were selected on the basis of their spherical morphology. In a double-blind experiment, their species identity and ability to coaggregate with human oral Actinomyces viscosus and Actinomyces naeslundii were determined. Of the 110 isolates characterized, 30 were identified as either Streptococcus mutans, Streptococcus anginosus-constellatus, or Veillonella parvula; none of these coaggregated with the actinomycetes. The remaining 80 isolates were identified as Streptococcus sanguis, Streptococcus mitis, Streptococcus MG-intermedius, or Streptococcus morbillorum. Of these 49 isolates (61%) coaggregated with actinomycetes, and nearly 90% (43 of 49 isolates) exhibited lactose-inhibitable coaggregations. Compared with previously characterized coaggregation properties determined with stock culture strains of streptococci, 82% of the fresh isolates exhibited identical coaggregations. The other 18% made up a new coaggregation group that possessed a related lactose-inhibitable coaggregation pattern. Thus, most fresh isolates that coaggregated exhibited lactose-inhibitable coaggregations with human oral actinomycetes. It is suggested that these coaggregations are mediated by a network of lectin-carbohydrate interactions similar to those already characterized in previous studies with stock cultures of actinomycetes and streptococci.

Actinomycetales↗

PubMed2004

Identification and characterization of a Neospora caninum microneme-associated protein (NcMIC4) that exhibits unique lactose-binding properties.

Microneme proteins have been shown to play an important role in the early phase of host cell adhesion, by mediating the contact between the parasite and host cell surface receptors. In this study we have identified and characterized a lectin-like protein of Neospora caninum tachyzoites which was purified by alpha-lactose-agarose affinity chromatography. Upon separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, this lactose-binding protein migrated at 70 and 55 kDa under reducing and nonreducing conditions, respectively. Immunofluorescence and immunogold electron microscopy with affinity-purified antibodies showed that the protein was associated with the tachyzoite micronemes. Mass spectrometry analyses and expressed sequence tag database mining revealed that this protein is a member of the Neospora microneme protein family; the protein was named NcMIC4 (N. caninum microneme protein 4). Upon two-dimensional gel electrophoresis, NcMIC4 separated into seven distinct isoforms. Incubation of extracellular parasites at 37 degrees C resulted in the secretion of NcMIC4 into the medium as a soluble protein, and the secreted protein exhibited a slightly reduced M(r) but retained its lactose-binding properties. Immunofluorescence was used to investigate the temporal and spatial distribution of NcMIC4 in tachyzoites entering their host cells and showed that reexpression of NcMIC4 took place 30 min after entry into the host cell. Incubation of secreted fractions and purified NcMIC4 with Vero cells demonstrated binding of NcMIC4 to Vero cells as well as binding to chondroitin sulfate A glycosaminoglycans.

Amino Acid Sequence↗

PubMed1974

Genetic evidence for the physiological significance of the D-tagatose 6-phosphate pathway of lactose and D-galactose degradation in staphylococcus aureus.

Mutants of Staphylococcus aureus were isolated which were unable to utilize d-galactose or lactose, but which were able to utilize all other carbohydrates tested. Growth of the mutants on a peptone-containing medium was inhibited by d-galactose. Of those mutants selected for further study, one (tagI2) was missing d-galactose 6-phosphate isomerase, one (tagK3) was missing d-tagatose 6-phosphate kinase, and one (tagA4) was missing d-tagatose 1, 6-diphosphate aldolase. Each of these mutants accumulated the substrate of the missing enzyme intracellularly. Spontaneous revertants of each of the mutants simultaneously regained their ability to utilize d-galactose and lactose, lost their sensitivity to d-galactose, regained the missing enzymatic activities, and no longer accumulated intermediates of the d-tagatose 6-phosphate pathway. These data support our previous contention that the physiologically significant route for the metabolism of d-galactose and the d-galactosyl moiety of lactose in S. aureus is the d-tagatose 6-phosphate pathway. Furthermore, a mutant constitutive for all three enzymes of this pathway was isolated, indicating that the products of the tagI, tagK, and tagA genes are under common genetic control. This conclusion was supported by the demonstration that d-galactose 6-phosphate isomerase, d-tagatose 6-phosphate kinase, and d-tagatose 1, 6-diphosphate aldolase are coordinately induced in the parental strain.

Aldehyde-Lyases↗

PubMed1974

Lactose permeation via the arabinose transport system in Escherichia coli K-12.

This paper describes the isolation and characterization of a mutant of Escherichia coli that transports lactose and its analog thiomethylgalactoside via the arabinose permeation system. Unlike transport via the lactose permease, this transport is not inhibited by thiodigalactoside, but was inhibited by arabinose, xylose, and fucose. The site of the mutation was in the arabinose C gene and confers constitutivity on the entire arabinose operon. Furthermore, this transport was found in 24 independently isolated arabinose-constitutive strains, and in strains which had been induced with arabinose and then starved to remove all traces of it. It was therefore concluded that lactose and thiomethylgalactoside are low-affinity substrates of at least one component of the normal arabinose permeation system.

Arabinose↗

PubMed1975

Induction of lactose transport in Escherichia coli during the absence of phospholipid synthesis.

Induction of lactose transport and of beta-galactosidase synthesis was examined in two Escherichia coli strains that require exogenous glycerol for phospholipid synthesis and growth. No preferential inhibition of lactose transport induction was observed when phospholipid synthesis was restricted to 5 to 10% of the normal rate. We conclude that the lactose transport system does not require concurrent phospholipid synthesis for its functional assembly.

Bacterial Proteins↗

PubMed1977

Pseudoreversion of lactose operator-constitutive mutants.

A set of pseudorevertants of lactose operator-constitutive (lacOc) mutant has been obtained. Analysis of a subset of these pseudorevertants indicates that, in some cases, the secondary mutation alters the lactose repressor (lacl gene product), whereas in others it seems to have occurred in the lactose operator (lacO) itself. Of the lacl gene mutations, the lacl8 mutation, already known to suppress all lacOc mutations nonspecifically, was recovered by a selection technique developed for this study. However, two additional lacl gene mutants were selected which appear to suppress lacOc sequences in a more-or-less specific fashion; repressor interaction with some operator sequences is facilitated, whereas the binding with lacO+ and others is attenuated concomitantly.

Escherichia coli↗

PubMed1978

Formylation of initiator tRNA methionine in procaryotic protein synthesis: in vivo polarity in lactose operon expression.

Eucaryotic and procaryotic organisms differ in two aspects of their translation machinery: polycistronic messengers are expressed as a sequence of individual proteins only in procaryotes, and the initiation of protein synthesis proceeds with an initiator tRNA which is found to be modified (formylated) in procaryotes and not in eucaryotes. In the present study, we show that formylation is required in vivo for the coordinate expression of the Escherichia coli lactose operon. Our experiments are consistent with a translation mechanism using dissociated ribosomes at the 5' end of the mRNA in a reaction that is only weakly dependent on formylation at this initiation step; the ribosomes then travel along the messenger and can reinitiate after the intracistronic barrier without dissociation. This latter initiation step is strongly dependent on the level of formylation: a low level of the formyl group, obtained by the antifolic agent trimethoprim, induces a strong polarity in the expression of the lactose operon. There exist mutant strains in which this polarity is much less apparent than in the wild type. We show here that such is the case of rpsL mutants. Ribosomes mutated in the S12 protein (rpsL) are found to be much more easily dissociated than the wild type. This might explain why the expression of the lactose operon on rpsL strains remains coordinated when the intracellular level of formylation is decreased.

Acetyltransferases↗