| InChI=1S/C7H14O6/c1-12-7-6(11)5(10)4(9)3(2-8)13-7/h3-11H,2H2,1H3/t3-,4-,5+,6-,7+/m1/s1 |
| HOVAGTYPODGVJG-ZFYZTMLRSA-N |
| CO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O |
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methyl α-D-glucopyranoside
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1-O-methyl-α-D-glucopyranose
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ChEBI
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1-O-methyl-α-D-glucopyranoside
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ChEBI
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1-O-methyl-α-D-glucoside
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ChEBI
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α-D-methyl glucoside
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ChEBI
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α-Methyl D-glucose ether
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NIST Chemistry WebBook
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alpha-Methyl-D-glucoside
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ChemIDplus
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alpha-Methylglucoside
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ChemIDplus
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Me α-Glc
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ChEBI
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Methyl alpha-D-glucoside
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ChemIDplus
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Methyl hexopyranoside
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NIST Chemistry WebBook
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81568
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Reaxys Registry Number
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Reaxys
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83829
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Gmelin Registry Number
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Gmelin
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97-30-3
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CAS Registry Number
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ChemIDplus
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97-30-3
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CAS Registry Number
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NIST Chemistry WebBook
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Paul A, Geetha M, Chacko BK, Appukuttan PS (2009)
Multiple specificity of human serum dextran-binding immunoglobulin: alpha (1-->6)- and beta (1-->3)-linked glucose and alpha (1-->3)-linked galactose in natural glycoconjugates are recognized.
Immunological investigations 38, 153-164 [PubMed:19330624]
[show Abstract]
Dextran-binding immunoglobulin (DIg) was detected in circulating immune complexes in young healthy blood donors. High molecular weight dextran or non-dialysable polysaccharides of edible sugar added to serum markedly increased DIg-containing immune complexes. DIg from plasma was purified by an improved affinity chromatography using Sephadex G-200 to increase yield. Recognition by DIg of alpha (1-->6) glucans in polystyrene-coated dextran was inhibited totally and its less avid recognition of beta (1-->3) glucans in yeast and barley partially by 50 mM 1-O-methyl-alpha-D-glucoside. All fractions of non-dialysable edible sugar separated by electrophoresis were recognized by DIg. While purified DIg contained nearly equal amounts of IgM and IgG, DIg in immune complexes isolated after addition of dextran to serum was 72% IgM. Recognition of bovine thyroglobulin, tumour laminin, and peanut-agglutinin-binding bovine heart glycoproteins, all containing terminal alpha (1-->3)-linked galactose epitopes, by DIg was inhibitable by 1-O-methyl-alpha-D-glucoside. Enzymatic removal or modification of the respective terminal alpha (1-->3)-linked galactose groups in these glycoproteins abolished their recognition by the antibody. Results suggest that DIg recognizes alpha (1-->6) glucans, alpha (1-->3) - linked galactose epitopes and less avidly beta (1-->3) glucans. Results also point to a new immunomodulatory effect of non-dialysable sugar and dietary beta-glucans. | Pikis A, Hess S, Arnold I, Erni B, Thompson J (2006)
Genetic requirements for growth of Escherichia coli K12 on methyl-alpha-D-glucopyranoside and the five alpha-D-glucosyl-D-fructose isomers of sucrose.
The Journal of biological chemistry 281, 17900-17908 [PubMed:16636060]
[show Abstract]
Strains of Escherichia coli K12, including MG-1655, accumulate methyl-alpha-D-glucopyranoside via the phosphoenolpyruvate-dependent glucose:phosphotransferase system (IICB(Glc)/IIA(Glc)). High concentrations of intracellular methyl-alpha-D-glucopyranoside 6-phosphate are toxic, and cell growth is prevented. However, transformation of E. coli MG-1655 with a plasmid (pAP1) encoding the gene aglB from Klebsiella pneumoniae resulted in excellent growth of the transformant MG-1655 (pAP1) on the glucose analog. AglB is an unusual NAD+/Mn2+-dependent phospho-alpha-glucosidase that promotes growth of MG-1655 (pAP1) by catalyzing the in vivo hydrolysis of methyl-alpha-D-glucopyranoside 6-phosphate to yield glucose 6-phosphate and methanol. When transformed with plasmid pAP2 encoding the K. pneumoniae genes aglB and aglA (an alpha-glucoside-specific transporter AglA (IICB(Agl))), strain MG-1655 (pAP2) metabolized a variety of other alpha-linked glucosides, including maltitol, isomaltose, and the following five isomers of sucrose: trehalulose alpha(1-->1), turanose alpha(1-->3), maltulose alpha(1-->4), leucrose alpha(1-->5), and palatinose alpha(1-->6). Remarkably, MG-1655 (pAP2) failed to metabolize sucrose alpha(1-->2). The E. coli K12 strain ZSC112L (ptsG::cat manXYZ nagE glk lac) can neither grow on glucose nor transport methyl-alpha-D-glucopyranoside. However, when transformed with pTSGH11 (encoding ptsG) or pAP2, this organism provided membranes that contained either the PtsG or AglA transporters, respectively. In vitro complementation of transporter-specific membranes with purified general phosphotransferase components showed that although PtsG and AglA recognized glucose and methyl-alpha-D-glucopyranoside, only AglA accepted other alpha-D-glucosides as substrates. Complementation experiments also revealed that IIA(Glc) was required for functional activity of both PtsG and AglA transporters. We conclude that AglA, AglB, and IIA(Glc) are necessary and sufficient for growth of E. coli K12 on methyl-alpha-D-glucoside and related alpha-D-glucopyranosides. | Strugala GJ, Elsenhans B, Forth W (2000)
Active transport inhibition in rat small intestine by amphiphilic amines: an in vitro study with various local anaesthetics.
Biochemical pharmacology 59, 907-913 [PubMed:10692555]
[show Abstract]
In the present investigation with rings of everted rat small intestine, amphiphilic amines such as local anaesthetics (e.g. lidocaine, procaine, tolycaine) were employed to study their effects on intestinal absorption of methyl alpha-D-glucoside, L-leucine, D-fructose, and 2-deoxy-D-glucose. All the amphiphilic amines tested, except for benzocaine, significantly inhibited Na(+)-dependent active uptake of methyl alpha-D-glucoside and L-leucine while leaving uptake of D-fructose (facilitated diffusion) and 2-deoxy-D-glucose (passive diffusion) unaffected. Increasing concentrations of lidocaine in the incubation medium inhibited the uptake of methyl alpha-D-glucoside (IC(50) approximately 3.5 mmol/L) and L-leucine (IC(50) approximately 6 mmol/L) in a dose-dependent manner. Complete reversibility of the inhibitory effect could only be achieved at short-term incubations ( | Vaughan HA, Loveland BE, Sandrin MS (1994)
Gal alpha(1,3)Gal is the major xenoepitope expressed on pig endothelial cells recognized by naturally occurring cytotoxic human antibodies.
Transplantation 58, 879-882 [PubMed:7524207]
[show Abstract]
Hyperacute rejection, mediated by natural antibody, is the major barrier to xenotransplantation. The studies reported herein were aimed at evaluating antibody-mediated cytotoxicity and the role of the Gal alpha(1,3)Gal epitope, which we had previously demonstrated was the major epitope of pig cells detected by naturally occurring human antibodies. Also, we had shown that this epitope could be induced in non-expressing cells by the transfection of a cDNA clone encoding alpha(1,3)galactosyl transferase, the enzyme that produces this epitope. The importance of the Gal alpha(1,3)Gal epitope was supported by (1) sugar inhibition studies; (2) complete absorption of cytotoxic antibodies by melibiose-sepharose columns; and (3) the ability of normal human serum to lyse COS cells after transfection with a cDNA clone encoding alpha(1,3)galactosyl transferase. These findings strongly suggest that the majority of cytotoxic human antibodies that would recognize a xenogeneic graft are directed to the Gal alpha(1,3)Gal epitope. | Sandrin MS, Vaughan HA, Dabkowski PL, McKenzie IF (1993)
Anti-pig IgM antibodies in human serum react predominantly with Gal(alpha 1-3)Gal epitopes.
Proceedings of the National Academy of Sciences of the United States of America 90, 11391-11395 [PubMed:7504304]
[show Abstract]
A major problem with pig-to-human-tissue xenograft studies is that humans have natural antibodies to pig cells; these antibodies would cause hyperacute rejection if pig tissues were xenografted to humans. Here we show that most of human IgM antibodies present in the serum of healthy donors and reactive with pig cells react with galactose in an (alpha 1-3) linkage with galactose--i.e., Gal(alpha 1-3)Gal. Absorption studies demonstrated that the antibodies detected the same or similar epitopes on the surface of pig erythrocytes, blood and splenic lymphocytes, and aortic endothelial cells (EC). The antibodies were sensitive to 2-mercaptoethanol (2ME) treatment, did not bind to protein A or G, and were present in the high molecular weight fraction of serum; they are clearly IgM antibodies. Further, the antibodies did not react with human ABO blood group substances and are not related to human blood group A or B, which carry a terminal galactose. The reaction of human serum with pig erythrocytes was specifically inhibited by mono- and disaccharides: D-galactose, melibiose, stachyose, methyl-alpha-D-galactopyranoside, and D-galactosamine but not by D-glucose or methyl-beta-D-galactopyranoside; demonstrating that the reaction is with galactose in an alpha and not a beta linkage. A cDNA clone encoding the murine alpha-1,3-galactosyltransferase (which transfers a terminal galactose residue with an (alpha 1-3) linkage to a subterminal galactose) was isolated by polymerase chain reaction (PCR), cloned, and transfected into COS cells, which are of Old World monkey origin and, like humans, do not express Gal(alpha 1-3)Gal. After transfection, COS cells became strongly reactive with human serum and with IB4 lectin [which reacts only with Gal(alpha 1-3)Gal]; this reactivity could be removed by absorption with pig erythrocytes. As most of the antibody reacting with pig cells can be removed by absorption with either melibiose or Gal(alpha 1-3)Gal+ COS cells, most of these react with Gal(alpha 1-3)Gal. These findings provide the basis for genetic manipulation of the pig alpha-1,3-galactosyltransferase for future transplantation studies. | Lostao MP, Berjón A, Barber A, Ponz F (1991)
On the multiplicity of glucose analogues transport systems in rat intestine.
Revista espanola de fisiologia 47, 209-216 [PubMed:1812543]
[show Abstract]
A study has been made to test if in intact epithelium of rat jejunum with in vivo and in vitro techniques, two transport systems for glucose and analogues, as those characterized in brush border membrane vesicles from guinea pig jejunum, are operative. The passive and mediated transport components of the D-galactose and methyl alpha-D-glucopyranoside intestinal absorption and the mutual inhibitions between both substrates at different relative concentrations have been measured. The effects of cytochalasin B and low temperature (20 degrees C) on the transport in vitro have also been observed. Cytochalasin B inhibits galactose and alpha-methylglucoside transport at 0.1 and 40 mM concentrations in similar percentage. Transport of 0.1 and 40 mM galactose is inhibited 61 and 77% respectively by low temperature (20 degrees C). The transport of galactose and alpha-methylglucoside could be explained by the assumption of just one transport system shared by both substrates, with a higher affinity for alpha-methylglucoside. Operation of two systems was not demanded by the results, due perhaps to species specificity or to the distorting action of the unstirred water layers. | Elsenhans B, Schümann K (1989)
In-vivo inhibition by polycations of small intestinal absorption of methyl alpha-D-glucoside and leucine in the rat.
Biochemical pharmacology 38, 3423-3429 [PubMed:2510735]
[show Abstract]
Polycations are able to inhibit active transport processes in rat small intestine in vitro. Whether this effect can also be confirmed in vivo is the concern of this study. Therefore, the effect of various polycations, e.g., protamine and polylysine, on the absorption of methyl alpha-D-glucoside and leucine was investigated in vivo by single-pass perfusion of rat jejunum. The inhibition of absorption of methyl alpha-D-glucoside and leucine by the polycations was strongly dose dependent. At a substrate concentration of 1 mmol/l a 50% inhibition was achieved with a protamine concentration of 3.2 mg/ml. The inhibition increased as the chain length of the polycation increased. In the presence of protamine the concentration-dependent leucine absorption was reduced at leucine concentrations below 60 mmol/l, but was increased at 100 mmol/l. Absorption of mannitol and 2-deoxy-D-glucose was significantly enhanced by the polycations. These results demonstrate that polycations inhibit active transport and increase passive diffusion processes in the rat small intestine in vivo. In addition, pretreatment of rats with a polycation added to the drinking water impaired the small intestinal absorption of methyl alpha-D-glucoside as subsequently measured by the tissue accumulation technique in vitro. Since polycations are hardly absorbed in the intestine, but do attach to negatively charged groups at the mucosal surface, polycations may be useful to study the influence of these negative groups on the absorption of nutrients and drugs. | Meadow ND, Revuelta R, Chen VN, Colwell RR, Roseman S (1987)
Phosphoenolpyruvate:glycose phosphotransferase system in species of Vibrio, a widely distributed marine bacterial genus.
Journal of bacteriology 169, 4893-4900 [PubMed:3667518]
[show Abstract]
The genus Vibrio is one of the most common and widely distributed groups of marine bacteria. Studies on the physiology of marine Vibrio species were initiated by examining 15 species for the bacterial phosphoenolpyruvate:glycose phosphotransferase system (PTS). All species tested contained a PTS analogous to the glucose-specific (IIGlc) system in enteric bacteria. Crude extracts of the cells showed immunological cross-reactivity with antibodies to enzyme I, HPr, and IIIGlc from Salmonella typhimurium when assayed by the rocket-line method. Toluene-permeabilized cells of 11 species were tested and were active in phosphorylating methyl alpha-D-glucoside with phosphoenolpyruvate but not ATP as the phosphoryl donor. Membranes from 10 species were assayed, and they phosphorylated methyl alpha-D-glucoside when supplemented with a phospho-IIIGlc-generating system composed of homogeneous proteins from enteric bacteria. Toluene-permeabilized cells and membranes of seven species were assayed, as were phosphorylated fructose and 2-deoxyglucose. IIIGlc was isolated from Vibrio fluvialis and was active in phosphorylating methyl alpha-D-glucoside when supplemented with a phospho-HPr-generating system composed of homogeneous proteins from Escherichia coli and membranes from either E. coli or V. fluvialis. These results show that the bacterial PTS is widely distributed in the marine environment and that it is likely to have a significant role in marine bacterial physiology and in the marine ecosystem. | Hollingsworth RI, Hrabak EM, Dazzo FB (1986)
Synthesis of 3,6-dideoxy-3-(methylamino)hexoses for g.l.c.-m.s. identification of Rhizobium lipopolysaccharide components.
Carbohydrate research 154, 103-113 [PubMed:3791291]
[show Abstract]
A direct synthetic route from methyl alpha-D-glucopyranoside to 3,6-dideoxy-3-(methylamino)hexoses having the D-gluco, D-galacto, and D-manno configurations has been developed. Methyl alpha-D-glucoside was converted into the 4,6-O-benzylidene-2,3-di-O-tosyl derivative, which was then transformed into the 4-O-benzyl-6-deoxy 2,3-ditosylate (5) by successive reductive cleavage of the acetal ring, iodination, and reduction. The intermediate 5 was readily converted into the allo 2,3-epoxide, which yielded the pivotal intermediate methyl 4-O-benzyl-3,6-dideoxy-3-(methylamino)-alpha-D-glucopyranoside (7) by cleavage of the oxirane ring with methylamine. The amino compound 7 can be directly converted into the derivatized galacto and manno derivatives for mass-spectrometric identification by selective inversion at C-4 and C-2, respectively, followed by hydrolysis, reduction, and acetylation. | Roth KS, Spencer PD, Higgins ES, Spencer RF (1985)
Effects of succinylacetone on methyl alpha-D-glucoside uptake by the rat renal tubule.
Biochimica et biophysica acta 820, 140-146 [PubMed:4052413]
[show Abstract]
Succinylacetone, a catabolic end-product of tyrosine, is excreted in large quantities in urine from individuals with hereditary tyrosinemia and the Fanconi syndrome. Succinylacetone inhibits rat renal tubular concentrative uptake of the glucose transport analogue, methyl alpha-D-glucoside, in a noncompetitive and reversible fashion. This compound also depresses oxygen consumption by the rat renal tubule without fine structural damage to mitochondria. It is concluded that succinylacetone may be a useful probe in elucidation of the biochemical mechanism underlying the human Fanconi syndrome. | Hsu BY, Marshall CM, Corcoran SM, Segal S (1982)
The effect of azaserine upon the proline and methyl alpha-D-glucoside transport systems of rat renal brush-border membranes.
Biochimica et biophysica acta 692, 41-51 [PubMed:7171588]
[show Abstract]
An inhibitory effect of azaserine on Na+ dependent proline and methyl alpha-D-glucoside transport of the rat renal brush-border membrane vesicles has been demonstrated. The inhibitory effects of azaserine were not the results of the drug disrupting the membrane vesicles as shown in osmolarity studies, nor did it affect the transport systems' affinities for Na+. Azaserine acts as a non-competitive inhibitor for the proline transport system in renal brush-border membranes by lowering 37% and 27% in the Vmax1 and Vmax2, respectively, when compared to that of control proline transport system. Azaserine had no effect upon the two Km values for proline uptake. Azaserine inhibition of methyl alpha-D-glucoside uptake by vesicles in the presence of 7.2 mM azaserine at 22 degrees C resulted in 66% increase in Km1 value and 44% decrease in Vmax1 as compared to that of control vesicles. There was no detectable effect upon the Km2 and Vmax2 of the methyl alpha-D-glucoside transport system. No effect of the drug was observed when sodium was equilibrated across the membrane, indicating that azaserine altered the driving force exerted by a sodium gradient. Azaserine only slightly affected the relative contribution of the two Km systems to total proline uptake. Contrary to the observed effect of azaserine upon the proline transport system, azaserine exerted a distinct effect upon the relative contribution to total uptake by the two Km systems in the low methyl alpha-D-glucoside concentration range. In the presence of 7.2 mM azaserine, the low-affinity, high-Km transport system becomes the major contributor to total methyl alpha-D-glucoside uptake by isolated renal brush-border vesicles. | Erlagaeva RS, Bolshakova TN, Shulgina MV, Bourd GI, Gershanovitch VN (1977)
Glucose effect in tgl mutant of Escherichia col K12 defective in methyl-alpha-D-glucoside transport.
European journal of biochemistry 72, 127-135 [PubMed:188655]
[show Abstract]
1. The dependence of the rate of accumulation of methyl-alpha-D-glucoside on its extracellular concentration was studied in the tgl mutant of Escherichia coli K12, isolated earlier. It has been shown that the kinetics of methyl-alpha-D-glucoside transport differ sharply from those in wild-type bacteria. 2. The beta-galactosidase synthesis in tgl strain is much less sensitive both to permanent and transient glucose catabolite repression. The level of cyclic AMP in mutant cells under the conditions of glucose catabolite repression is several times higher than in the parent strain. 3. The tgl mutation does not affect the manifestation of catabolite inhibition and inducer exclusion with glucose. 4. The data obtained are discussed in the light of a hypothesis concerning the existence of two sites, binding and pecific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system. The tgl mutation alters the first site, and the second one is damaged by the pgt mutation. 5. It is suggested that the products of the tgl and gpt genes are necessary for the manifestation of the phenomena of glucose permanent and transient repression. The effects of catabolite inhibition and inducer exclusion are realized irrespective of the existence or absence of the tgl product. | Reizer J, Thalenfeld B, Grossowicz N (1976)
Methyl-alpha-D-glucoside uptake and splitting by a thermophilic bacillus.
Nature 260, 433-435 [PubMed:1256584] | Harris P, Miller EK (1976)
Growth of bacilli on methyl-alpha-D-glucoside.
Nature 260, 432-433 [PubMed:815827] | Bourd GI, Erlagaeva RS, Bolshakova TN, Gershanovitch VN (1975)
Glucose catabolite repression in Escherichia coli K12 mutants defective in methyl-alpha-d-glucoside transport.
European journal of biochemistry 53, 419-427 [PubMed:1095369]
[show Abstract]
1. Two spontaneous Escherichia coli K12 mutants resistant to glucose catabolite repression were isolated using minimal agar plates with methyl alpha-D-glucoside. Mutants grow well on glucose and mannitol. 2. Glucose does not inhibit the inducible enzyme synthesis in isolated mutants: mutant cell (in contrast to parent cells) produce high levels of beta-galactosidase and L-tryptophanase under the conditions of glucose catabolite repression. 3. The isolated mutants are negative in methyl-alpha-D-glucoside transport; glucose uptake is not severely damaged. But the mutants (named tgl, transport of glucose) retained the ability to phosphorylate methyl alpha-D-glucoside in vitro at the expense of phosphoenolpyruvate. 4. The tgl mutation is cotransduced with purB and pyrC markers, i.e. locates near 24 min of the E. coli chromosome map. 5. It is thought that E. coli cells possess two glucose transport systems. The first one is represented by the glucose-specific enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system. The second glucose transport system (coded for tgl gene) functions as permease and possesses high affinity to methyl alpha-D-glucoside. The integrity of glucose permease determine the sensitivity of the cell to glucose catabolite repression. | Matsumoto K, Iuchi S, Fujisawa A, Tanaka S (1974)
Enrichment of mutants lacking the phosphoenolpyruvate-dependent phosphotransferase system of Vibrio parahaemolyticus by screening with methyl-alpha-D-glucoside.
Journal of bacteriology 119, 632-634 [PubMed:4851869]
[show Abstract]
Screening with methyl-alpha-d-glucoside was an efficient procedure for enrichment of mutants lacking the glucose transport system and of the pleiotropic mutants lacking the phosphoenolpyruvate-dependent phosphotransferase system in Vibrio parahaemolyticus. |
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