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PubMed1979

Sucrose transport by the Escherichia coli lactose carrier.

Several lines of evidence suggest that sucrose is transported by the lactose carrier of Escherichia coli. Entry of sucrose was monitored by an osmotic method which involves exposure of cells to a hyperosmotic solution of disaccharide (250 mM). Such cells shrink (optical density rises), and if the solute enters the cell, there is a return toward initial values (optical density falls). By this technique sucrose was found to enter cells at a rate approximately one third that of lactose. In addition, the entry of [14C]sucrose was followed by direct analysis of cell contents after separation of cells from the medium by centrifugation. Sucrose accumulated within the cell to a concentration 160% of that in the external medium. The addition of sucrose to an anaerobic suspension of cells resulted in a small alkalinization of the external medium. These data are consistent with the view that the lactose carrier can accumulate sucrose by a proton cotransport system. The carrier exhibits a very low affinity for the disaccharide (150 mM) but a moderately rapid Vmax.

Biological Transport, Active↗

PubMed1983

Regulation of lactose-phosphoenolpyruvate-dependent phosphotransferase system and beta-D-phosphogalactoside galactohydrolase activities in Lactobacillus casei.

The lactose-phosphoenolpyruvate-dependent phosphotransferase system (lac-PTS) and beta-D-phosphogalactoside galactohydrolase (P-beta-gal) mediate the metabolism of lactose by Lactobacillus casei. Starved cells of L. casei contained a high intracellular concentration of phosphoenolpyruvate, and this endogenous energy reserve facilitated characterization of phosphotransferase system activities in physiologically intact cells. Data obtained from transport studies with whole cells and from in vitro phosphotransferase system assays with permeabilized cells revealed that the lac-PTS had a high affinity for beta-galactosides (e.g., lactose, lactulose, lactobionic acid, and arabinosyl-beta-D-galactoside). lac-PTS and P-beta-gal activities were determined in wild-type strains and strains defective in the glucose-phosphoenolpyruvate-dependent phosphotransferase system after growth on various sugars and in the presence of potential inducers. We found that (i) the lac genes (i.e., the genes coding for the lac-PTS proteins and P-beta-gal) were induced by metabolizable and non-metabolizable beta-galactosides (presumably acting as their phosphorylated derivatives), (ii) galactose 6-phosphate was not an inducer in most strains, (iii) the ratio of lac-PTS activity to P-beta-gal activity in a given strain was not constant, and (iv) inhibition of lac gene expression during growth on glucose was a consequence of glucose-phosphoenolpyruvate-dependent phosphotransferase system-mediated inducer exclusion, repressive effects of a functional glucose-phosphoenolpyruvate-dependent phosphotransferase system and glucose-derived metabolites. The expression of the lac-PTS structural genes and the expression of the P-beta-gal gene are independently regulated and may be subject to both positive control and negative control.

Enzyme Induction↗

PubMed1991

The binding of cyclic AMP receptor protein to two lactose promoter sites is not cooperative in vitro.

The lactose promoter-operator region of Escherichia coli contains two binding sites for cyclic AMP receptor protein (CAP), two for the lactose repressor, and two for RNA polymerase. The high density of binding sites makes cooperative interactions between these proteins likely. In this study, we used the gel electrophoresis mobility shift assay and binding partition analysis techniques to determine whether the secondary CAP site influences the binding of CAP to the principal CAP site in the lactose promoter when both are present on a linear DNA molecule. Such an effect could occur through the formation of a bridged DNA-CAP-DNA structure, through the interaction of CAP molecules bound to each of the sites, or through allosteric effects caused by CAP-mediated DNA bending. We found, however, that the interaction of CAP with these sites was not cooperative, indicating that CAP sites 1 and 2 bind CAP in an independent manner.

Base Sequence↗

PubMed1992

Amino acid substitution in the lactose carrier protein with the use of amber suppressors.

Five lacY mutants with amber stop codons at known positions were each placed into 12 different suppressor strains. The 60 amino acid substitutions obtained in this manner were tested for growth on lactose-minimal medium plates and for transport of lactose, melibiose, and thiomethylgalactoside. Most of the amino acid substitutions in the regions of the putative loops (between transmembrane alpha helices) resulted in a reasonable growth rate on lactose with moderate-to-good transport activity. In one strain (glycine substituted for Trp-10), abnormal sugar recognition was found. The substitution of proline for Trp-33 (in the region of the first alpha helix) showed no activity, while four additional substitutions (lysine, leucine, cysteine, and glutamic acid) showed low activity. Altered sugar specificity was observed when Trp-33 was replaced by serine, glutamine, tyrosine, alanine, histidine, or phenylalanine. It is concluded that Trp-33 may be involved directly or indirectly in sugar recognition.

Amino Acid Sequence↗

PubMed2002

Galactose and lactose genes from the galactose-positive bacterium Streptococcus salivarius and the phylogenetically related galactose-negative bacterium Streptococcus thermophilus: organization, sequence, transcription, and activity of the gal gene products.

Streptococcus salivarius is a lactose- and galactose-positive bacterium that is phylogenetically closely related to Streptococcus thermophilus, a bacterium that metabolizes lactose but not galactose. In this paper, we report a comparative characterization of the S. salivarius and S. thermophilus gal-lac gene clusters. The clusters have the same organization with the order galR (codes for a transcriptional regulator and is transcribed in the opposite direction), galK (galactokinase), galT (galactose-1-P uridylyltransferase), galE (UDP-glucose 4-epimerase), galM (galactose mutarotase), lacS (lactose transporter), and lacZ (beta-galactosidase). An analysis of the nucleotide sequence as well as Northern blotting and primer extension experiments revealed the presence of four promoters located upstream from galR, the gal operon, galM, and the lac operon of S. salivarius. Putative promoters with virtually identical nucleotide sequences were found at the same positions in the S. thermophilus gal-lac gene cluster. An additional putative internal promoter at the 3' end of galT was found in S. thermophilus but not in S. salivarius. The results clearly indicated that the gal-lac gene cluster was efficiently transcribed in both species. The Shine-Dalgarno sequences of galT and galE were identical in both species, whereas the ribosome binding site of S. thermophilus galK differed from that of S. salivarius by two nucleotides, suggesting that the S. thermophilus galK gene might be poorly translated. This was confirmed by measurements of enzyme activities.

Base Sequence↗

PubMed1969

Kinetics of induction of the lactose operon on an episome in Samonellla typhimurium.

A kinetic study of induction of the enzymes of the lactose operon was carried out under conditions known to affect the kinetics of derepression of the enzymes of the histidine operon. The results show that the lactose system is similar to the histidine system in its responsiveness to conditions thought to affect the formylating capacity of the cell. This was demonstrated in the following ways: (i) trimethoprim, which is known to reduce the formylating capacity of the cell, gives rise to a relatively long interval between the times of induction of beta-galactosidase and transacetylase; (ii) under conditions in which the histidine operon is derepressed, chloramphenicol causes a prolongation of the interval between the times of induction of the two enzymes, and this prolongation is reversed by adenine, methionine, and serine, compounds known to enrich the one-carbon pool of the cell; and (iii) 4-amino-5-imidazolcarboxamide ribonucleoside, a compound which may act as a drain for formyl groups, reverses the effect of the latter compounds. The finding that the interval between the times of induction of the two enzymes is shortened under conditions expected to maintain a relatively high intracellular fo rmylating capacity suggests that under certain conditions translation of the polycistronic messenger ribonucleic acid of the lactose operon may be initiated at more than one site or may proceed more rapidly from the operator end.

Acyltransferases↗

PubMed1987

Bacteremia caused by a lactose-fermenting, multiply resistant Salmonella typhi strain in a patient recovering from typhoid fever.

A female patient suffered a typical attack of typhoid fever due to a lactose-negative, fully susceptible Salmonella typhi strain. During convalescence she became febrile, and a lactose-fermenting S. typhi strain resistant to ampicillin, chloramphenicol, tetracycline, and trimethoprim was isolated from blood culture. This isolated was shown to harbor a plasmid which cotransferred lactose fermentation and antibiotic resistance.

Adolescent↗

PubMed1987

Lactose malabsorption in Polynesian and white children in the south west Pacific studied by breath hydrogen technique.

Lactose malabsorption was studied by a breath hydrogen technique in 139 Samoan and 68 white schoolchildren. The Samoans were studied in four locations, two in Western Samoa and two in New Zealand, and the white children in both the Cook Islands and New Zealand. The prevalence of malabsorption varied with location: for Samoans it ranged from 41% to 60% in Western Samoa and 0% to 35% in New Zealand; white children had rates of 27% in the Cook Islands and 5% in New Zealand. Environmental factors rather than genetic factors are likely to play the main part in initiating if not perpetuating lactose malabsorption. In both races lactose malabsorption had no effect on the acceptance of, consumption of, and number of gastrointestinal symptoms caused by milk and milk biscuits. Children who had symptoms after consuming a particular dairy product were more likely to say they disliked it than those who reported no symptoms.

Adolescent↗

PubMed1978

The metabolism of carbohydrates by extremely halophilic bacteria: the identification of lactobionic acid as a product of lactose metabolism by Halobacterium saccharovorum.

Nongrowing cells of Halobacterium saccharovorum oxidized lactose to a product identified as lactobionic acid by thin-layer, paper, and column chromatography, and by identification of the galactose and gluconic acid produced from it after acid hydrolysis. Growing cells oxidized lactose to a product that was identical with lactobionate except that it did not serve as a substrate for galactose oxidase. While the identity of this compound has not been established, it is suggested that the product is lactobionic acid in which the galactose moeity is in the furanose form. Neither lactobionate nor the product produced by growing cells was further metabolized, suggesting that lactose oxidation is not coupled to growth.

Cells, Cultured↗

PubMed2000

Use of lactose to induce expression of soluble NifA protein domains of Herbaspirillum seropedicae in Escherichia coli.

Overexpression and purification are procedures used to allow functional and structural characterization of proteins. Many overexpressed proteins are partially or completely insoluble, and can not be easily purified. The NifA protein is an enhancer-binding protein involved in activating the expression of nif and some fix genes. The NifA protein from many organisms is usually insoluble when over-expressed, and therefore difficult to work with in vitro. In this work we have overexpressed the central + C-terminal and the central domains of the Herbaspirrilum seropedicae NifA protein in an Escherichia coli background. Expression was induced with either IPTG or lactose. The data showed that induction with lactose promoted a significantly higher percentage of these proteins in the soluble fraction than with IPTG. This probably reflects a slower kinetics of induction by lactose.

Bacterial Proteins↗

PubMed2005

Dietary protein and lactose increase translation initiation factor activation and tissue protein synthesis in neonatal pigs.

Protein synthesis and eukaryotic initiation factor (eIF) activation are increased in muscle and liver of pigs parenterally infused with amino acids and insulin. To examine the effects of enteral protein and carbohydrate on protein synthesis, pigs (n = 42, 1.7 kg body wt) were fed isocaloric milk diets containing three levels of protein (5, 15, and 25 g x kg body wt(-1) x day(-1)) and two levels of lactose (low = 11 and high = 23 g x kg body wt(-1) x day(-1)) from 1 to 6 days of age. On day 7, pigs were gavage fed after 4-h food deprivation, and tissue protein synthesis rates and biomarkers of mRNA translation were assessed. Piglet growth and protein synthesis rates in muscle and liver increased with dietary protein and plateaued at 15 g x kg body wt(-1) x day(-1) (P < 0.001). Growth tended to be greater in high-lactose-fed pigs (P = 0.07). Plasma insulin was lowest in pigs fed 5 g x kg body wt(-1) x day(-1) protein (P < 0.0001). Plasma branched-chain amino acids increased as protein intake increased (P < 0.0001). Muscle (P < 0.001) and liver (P < or = 0.001) ribosomal protein S6 kinase-1 and eIF4E-binding protein phosphorylation increased with protein intake and plateaued at 15 g x kg body wt(-1) x day(-1). The results indicate that growth and protein synthesis rates in neonatal pigs are influenced by dietary protein and lactose intake and might be mediated by plasma amino acids and insulin levels. However, feeding protein well above the piglet's requirement does not further stimulate the activation of translation initiation or protein synthesis in skeletal muscle and liver.

Administration, Oral↗

PubMed1982

Metabolic effects produced in baboons associated with the ingestion of diets based on lactose hydrolysate.

Diets containing 80% by weight carbohydrate provided by lactose hydrolysate (prepared by two different techniques), sucrose or glucose were given to baboons for 10-week periods. Fasting blood samples were taken regularly and the serum was assayed for galactose, glucose, insulin, triglyceride and cholesterol. The body weight of the animals was recorded. During both lactose hydrolysate dietary periods the mean fasting serum galactose concentration increased whereas the fasting serum glucose level fell initially. The fasting serum glucose concentration rose with both the glucose and the sucrose diets. The fasting serum triglyceride concentration of the female baboons increased significantly during both periods of ingestion of lactose-hydrolysate-based diets whereas the glucose and sucrose diets did not produce a significant effect. The sucrose diet produced a consistent increase in the mean triglyceride level of the male baboons. The mean serum cholesterol fell in the male and female baboons during all four diets.

Animals↗

PubMed1985

Variations of lactose and oligosaccharides in milk from women of blood types secretor A or H, secretor Lewis, and secretor H/nonsecretor Lewis during the course of lactation.

Variations of lactose and oligosaccharides in human milk were studied over a 3-month lactation period by dialysis, chromatography on Bio-gel P-2 column, paper chromatography, colorimetric analysis and gas chromatography. Milk samples were collected from donors of various blood and secretor types. An increase in the concentration of lactose was noted: 59.25 +/- 1.61 to 72.17 +/- 1.35 g/l for the group of secretor A secretor Lea Leb individuals, and from 62.25 +/- 1.35 to 73.15 +/- 3.45 g/l for the group of secretor H secretor Lea Leb individuals. A decrease in the concentration of oligosaccharides was also found: from 16.71 +/- 0.99 to 7.90 +/- 1.29 g/l and from 18.51 +/- 0.74 to 7.33 +/- 0.65 g/l, respectively, for these same groups. In secretor H nonsecretor Lewis individuals, the concentration of lactose increased from 67.97 +/- 3.09 to 77.42 +/- 1.88 g/l, and the concentration of oligosaccharides decreased from 13.27 +/- 0.40 to 3.47 +/- 0.33 g/l. Analysis of oligosaccharide composition by chromatography showed that variations are in relation to the secretor Lewis type. All oligosaccharides decreased equally throughout the lactation period, regardless of the blood group. The decrease was more rapid, however, in the nonsecretor Lewis individuals. In these individuals, the absence of certain oligosaccharides is not compensated by an overproduction of the other oligosaccharides present or by biosynthesis of structurally different oligosaccharides. The origin of these oligosaccharides is discussed.

ABO Blood-Group System↗

PubMed1977

Failure of lactose and glucose to influence in vivo intestinal calcium transport in normal rats.

The influence of luminal lactose and glucose on intestinal calcium transport was examined in vivo in normal post-weaned young rats. In situ segments of duodenum, midgut and ileum were perfused through the lumen for 1 h with an isotonic solution of 3.4 mM calcium containing radioactive isotopic 45Ca as tracer and additionally either 10 mM lactose or 10 mM glucose, or, for the control group, no saccharide. Net absorption was measured by disappearance of luminal calcium; lumen-to-plasma flux was determined from the disappearance of tracer 45Ca. This concentration of luminal lactose or glucose had no direct effect on calcium transport under these steady state conditions.

Animals↗

PubMed1997

Lactose-intolerance may induce severe chronic eczema.

The primary acquired lactase deficiency of the adult is known to cause various disturbances in the gastrointestinal tract while extraintestinal symptoms are unusual. Here we report on a histologically proven chronic eczema requiring corticosteroid treatment for several months. It was obviously induced by a concomitant lactose intolerance since the introduction of a lactose-free diet led to a complete disappearance of the eczema and allowed the discontinuation of the corticosteroid treatment. As far as we know, this is the first case report of an eczema caused by a lactose intolerance.

Adrenal Cortex Hormones↗

PubMed1980

Lactose malabsorption in two sibling rhesus monkeys (Macaca mulatta).

Observation of two sibling rhesus monkeys, Macaca mulatta, indicated that they were intolerant to lactose. While on a lactose formula the monkeys had severe diarrhea and weight loss but were otherwise healthy. When a lactose-free formula was instituted, the diarrhea abated and there was a steady weight gain.

Animals↗

PubMed1983

Urogastrone and lactose concentrations in precolostrum, colostrum, and milk.

The concentration of urogastrone (URO) and lactose was measured in breast secretions from four women. URO levels were high in precolostrum and fell markedly around the time of parturition to relatively constant low levels in mature milk. When milk samples were fractionated on a Biogel P10 column, the major peak of immunoreactivity occurred at the point at which pure URO eluted. There was good correspondence between the fall in URO levels at birth and the increase in lactose levels, suggesting that the decrease in URO was a dilution effect as the osmotic influence of lactose increased.

Colostrum↗

PubMed2006

Relationship between calcium, lactose, vitamin D, and dairy products and ovarian cancer.

Few prospective studies of the relationship between intake of dairy foods, calcium, vitamin D, and lactose and ovarian cancer have been conducted, and results have been largely inconsistent. Two recent studies found significant increased risk with frequent dairy consumption and perhaps with high intakes of calcium or lactose. The authors investigated the association between these foods and nutrients and ovarian cancer risk among 31,925 subjects in the Breast Cancer Detection Demonstration Project follow-up cohort. Multivariable (MV) relative risks (RRs) adjusted for age, parity, and other factors were estimated using Cox proportional hazards models. Over an average follow-up of 8.3 yr, 146 incident ovarian cancer cases were confirmed. Higher intakes of total dairy food (comparing four or more servings per day vs. less than one serving per day) were associated with a statistically significant decreased risk of ovarian cancer, although the trend was not significant (MV RR = 0.42; 95% confidence interval (CI) = 0.20-0.89; P for trend = 0.07). Comparing extreme quartiles, we observed a statistically nonsignificant inverse association between high dietary calcium intake and ovarian cancer (RR = 0.67; 95% CI = 0.43, 1.04; P for trend = 0.08). No statistically significant relations were found for consumption of specific dairy foods, lactose, or vitamin D and ovarian cancer risk. The possibility of a decreased risk of ovarian cancer for dietary calcium merits further evaluation.

Calcium, Dietary↗