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

---

Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Endo-beta-galactosidase, a glycosidase that hydrolyzes Gal beta 1-4 GlcNAc linkages in glycoconjugates, has been used to probe the plasma membrane of human erythrocytes. Coomassie blue staining of stroma components separated by sodium dodecyl sulfate-acrylamide gel electrophoresis indicates that treatment of red cells with endo-beta-galactosidase converts Protein 3, the anion transporter of the erythrocyte, to a more compact staining band. No other components detected by Coomassie staining are affected. Following labeling of red cells with galactose oxidase + NaB3H4, 45 to 50% of the [3H]galactose residues can be released by endo-beta-galactosidase. In contrast, only 5% of the label incorporated by treatment with periodate + NaB3H4, can be removed. [3H]Galactose residues are released from three components: Protein 3, Band 4.5, and the megaloglycolipids. The susceptibility of these components to endo-beta-galactosidase, together with the high content of Gal and GlcNAc present in Protein 3 and the megaloglycolipids, suggests that the erythrocyte membrane contains several components with N-acetyllactosamine repeating units, a structure commonly found in connective tissue glycoconjugates.
...
PMID:Effect of endo-beta-galactosidase on intact human erythrocytes. 11 98

Human lymphocyte cultures produced large amounts of interferon after treatment with the enzyme galactose oxidase. Interferon production was detectable as early as 3 h after enzymatic treatment and reached a level of about 10(4) reference units 20 to 24 h later. Galactose oxidase-induced interferon appeared to be immune interferon on the basis of acid lability, lack of neutralization by antibody to leukocyte interferon, and slow kinetics of activation of the cellular antiviral state. Interferon production was inhibited to the same extent (99%) by pretreatment of the cells with beta-galactosidase or with neuraminidase followed by beta-galactosidase, suggesting that the critical event for activation of interferon production is the oxidation of exposed galactose residues on lymphocyte membrane.
...
PMID:Enzymatic induction of interferon production by galactose oxidase treatment of human lymphoid cells. 11 35

A protein, present in bovine seminal plasma, initiates forward motility in immature, immotile caput spermatozoa that have been incubated with a cyclic AMP phosphodiesterase inhibitor. An improved motility assay was developed to study this process and the protein involved. This forward motility protein exhibits multiple forms when fractionated on the basis of charge or molecular weight. Molecular sieving in urea or sodium dodecyl sulfate and dithiothreitol results in a single peak of activity which will re-form the larger aggregates in the absence of these agents. The molecular weight of this monomeric motility protein, as estimated from molecular sieving under these dissociating conditions, is 37,500. The forward motility protein can be partially purified by heat treatment, gell chromatography in urea, and affinity chromatography on concanavalin A/agarose. Enzymatic treatments further suggest a glycoprotein nature, i.e. treatment with beta-galactosidase, neuraminidase, alpha-mannosidase, or galactose oxidase reduces its activity by 50%; treatment with trypsin completely abolishes forward motility protein activity. On the basis of concurrent studies on the activity, properties, and distribution of forward motility protein in bovine body fluids, it is suggested that this protein is involved in the development of the capacity for motility as sperm traverse the epididymis.
...
PMID:Bovine sperm forward motility protein. Partial purification and characterization. 21 Nov 30

Using galactose oxidase as well as beta-galactosidase to produce modifications of the galactose units, the functional significance of these carbohydrate residues on the coagulant activity of bovine Factor V glycoprotein was evaluated. Incubation of native Factor V with galactose oxidase or hydrolysis of asialo-Factor V with beta-galactosidase results in a loss of Factor V activity. The inactivation of Factor V by oxidation of galactose moieties is partially reversible upon reduction of the newly formed aldehyde groups with sodium borohydride. The extent of reversal depends upon the degree of inactivation achieved. Thus, Factor V which retained 30% of the original activity following galactose oxidation returns to 75% of the original coagulant activity upon borohydride reduction; but, after destruction of 85% of the original activity treatment with borohydride returns to about 30%. In the initial stages of the inactivation of Factor V by treatment with galactose oxidase, the loss of Factor V coagulant activity is directly proportional to the moles of galactose oxidized. However, as the reaction progresses, the rate of galactose oxidation exceeds the rate of loss of Factor V activity. Moreover, galactose oxidation continues even after complete inactivation of Factor V. These results suggest that the galactose residues most susceptible to attack by galactose oxidase are those necessary for the activity of this coagulant protein. Only 15 galactose residues/mol of Factor V are susceptible to galactose oxidase prior to removal of sialic acid. In contrast, 37 galactose residues/mol of Factor V are found after acid hydrolysis. These results suggest that Factor V glycoprotein contains more than one type of sialyl-galactose linkages, the C2,3 or C2,4 linkages susceptible to oxidation in the native protein and the C2,6 linkage which is resistant. Native Factor V binds with diarachidonyl lecithin forming an active complex of lower buoyant density, while the Factor V oxidized with galactose oxidase does not. The Factor V-phospholipid complex is protected from inactivation by galactose oxidase. Moreover, lipid binding diminishes the extent of oxidation of galactose residues. Certain galactose groups are essential for coagulant activity probably because they are required for binding to phospholipid, a prerequisite to Factor V action.
...
PMID:Role of galactose in bovine factor V. 117 64

Peanut agglutinin, purified by affinity chromatography, agglutinates lymphocytes from mouse, rat, guinea pig, and man only after their treatment with neuraminidase. However, it stimulates only neuraminidase-treated rat and human cells. A similar number cell surface receptors for peanut agglutinin was found on neuraminidase-treated rat and mouse lymphocytes although the latter cells were not stimulated by the lectin. Galactose specifically inhibited the agglutination and stimulation of lymphocytes by peanut agglutinin. Sequential treatment of lymphocytes with neuraminidase and beta-galactosidase markedly reduced the response of the cells to stimulation by peanut agglutinin, soybean agglutinin, and galactose oxidase. It is suggested that the same galactosyl residue may be the target for the initial step in triggering lymphocytes by the above mentioned mitogens.
...
PMID:Peanut agglutinin, a new mitogen that binds to galactosyl sites exposed after neuraminidase treatment. 117 75

Rhodopsin's oligosaccharide chains contain predominantly two types of sugar residues: mannose and N-acetylglucosamine. In the present work, bovine and rat rhodopsin were analysed biochemically for the presence of a third sugar, galactose. Treatment of bovine rod outer segments (ROS) with galactose oxidase followed by reduction with tritium-labeled sodium borohydride revealed the presence of existing molecules of galactose on rhodopsin. Rats injected intravitreally with [3H]galactose and [14C]leucine and maintained in darkness were killed 1 hr, 6 hr, 1, 3 or 5 days following the injection. Retinas were collected for subcellular fractionation and rhodopsin from each of the fractions was purified by ConA sepharose chromatography and SDS-PAGE. During the first 6 hr, galactose selectively labeled rhodopsin in the Golgi-enriched fraction resulting in increased [3H]/[14C] ratios in both Golgi and ROS. The data suggested that trimming was occurring at the transition from Golgi to ROS. Furthermore, a decrease in isotope ratio in the ROS between 6 hr and 1 day suggested further trimming of rhodopsin after membrane assembly in the ROS. Additional in vivo experiments demonstrated existing molecules of galactose on rhodopsin's oligosaccharide chain using lectin affinity chromatography. Rats injected intravitreally with [35S]methionine were dark-adapted for 2 hr. Following subcellular fractionation of retinas, ConA purified rhodopsin from ROS was applied to one of two additional lectin columns: Ricinus communis agglutinin (RCA) or Griffonia simplicifolia I (GSA). Eight to nine percent of the labeled rhodopsin was bound to and eluted from RCA, whereas none bound to GSA, indicating the presence of a beta-galactoside. The RCA agarose eluted protein co-electrophoresed with a rhodopsin standard and was light sensitive. Galactose was shown to be the terminal sugar on this subset of rhodopsin and was not capped by neuraminic acid. Binding of rhodopsin's oligosaccharide to RCA was abolished by pre-treatment with beta-galactosidase. Decreased binding of rhodopsin to RCA was observed following intravitreal injection of castanospermine but not swainsonine. Of those two inhibitors of glycoprotein trimming, only castanospermine would be expected to prevent the addition of galactose to the oligosaccharide. The association of galactose with rat rhodopsin appeared to be a transient one. At 2 hr, 8-9% of rhodopsin contained galactose, at 6 hr only 2.2% had galactose and by 24 hr less than 1% did. The galactose was trimmed from rhodopsin's oligosaccharide presumably after its role was complete. Separation of rhodopsin of the plasma membranes from rhodopsin of discs indicated that 75% of the galactose-containing rhodopsin was in the plasma membrane and only 25% was in the discs. These findings suggested a possible role for galactose in new disc formation with subsequent removal after the discs are sealed.
...
PMID:Transient hyperglycosylation of rhodopsin with galactose. 193 88

The structure of the N-linked oligosaccharide of the 85-kDa surface glycoprotein (Tc-85) from the infective trypomastigote form of Trypanosoma cruzi was investigated. Tc-85 metabolically labeled with [14C]glucose was purified by affinity chromatography on wheat germ agglutinin-Sepharose. Binding to the lectin was lost on treatment of Tc-85 with neuraminidase. The N-linked asialo-oligosaccharide was released by endo-beta-N-acetylglucosaminidase F digestion of asialo-Tc-85 and was further analyzed using specific exoglycosidases. [14C]fucose was detected after alpha-L-fucosidase treatment or mild acid hydrolysis. The afucosyl oligosaccharide was 3H-labeled by the galactose oxidase-NaB3H4 method. [3H]Galactose was released by alpha-galactosidase, and only then was beta-galactosidase effective in removing another galactose. The gal(alpha 1-3)gal unit was demonstrated by periodate oxidation studies on the [3H]galactose-labeled asialo-glycoprotein. The presence of gal(alpha 1-3)gal in Tc-85 could be related to the recent finding of elevated antibody levels against this epitope in patients with Chagas' disease.
...
PMID:The N-linked carbohydrate chain of the 85-kilodalton glycoprotein from Trypanosoma cruzi trypomastigotes contains sialyl, fucosyl and galactosyl (alpha 1-3)galactose units. 210 74

The ability of von Willebrand factor protein (vWF) to agglutinate platelets with ristocetin depends upon the presence of its highest molecular weight multimers (HMWM) and its intact carbohydrate structure. Previously we demonstrated that the HMWM are preferentially adsorbed to purified fibrillar type I collagen. The role of the carbohydrate structure of vWF in this function has not been established. In these studies complete desialylation (greater than 95%) of the intact protein by neuraminidase did not interfere with the normal adsorption of vWF activity to type I collagen. In contrast, modification of the penultimate galactose of the desialylated protein with galactose oxidase or beta-galactosidase markedly reduced adsorption of vWF activity by collagen. Subsequent reduction of the oxidized desialylated protein with potassium borohydride completely regenerated the normal adsorption of vWF activity by collagen. Enzymatic modification of the penultimate galactose moiety of vWF resulted in a loss of the HMWM, as observed following SDS-glyoxyl agarose electrophoresis. This was in contrast to desialylated vWF, which appeared intact structurally and which predictably lost its HMWM upon exposure to collagen in a manner similar to native vWF. Therefore, the carbohydrate structure of vWF and, in particular, the penultimate galactose moiety, may be critical for vWF-collagen interactions and for the mediation of primary hemostasis.
...
PMID:Critical role of the carbohydrate moiety in human von Willebrand factor protein for interactions with type I collagen. 230 Sep 25

Two monoclonal antibodies, NCC-LU-35 and NCC-LU-81, have been established after immunization of mice with membrane preparations of human lung cancer Lu65 tumor xenograft cells grown in vivo and intact cells cultured in vitro, respectively. These two antibodies react specifically with a majority of human adenocarcinomas, irrespective of the host's blood group ABO status, as well as with normal tissues and erythrocytes of blood group A individuals. The antigenicity is associated with a high molecular weight mucin-like glycoprotein separated by gel filtration of Lu65 tumor extracts. The epitope of the mucin-like glycoprotein has been identified as alpha-N-acetylgalactosaminyl residue directly linked O-glycosidically to serine or threonine residues of polypeptides. This epitope was serologically detected several years ago and given the name Tn. Our identification of the epitope is based on the following results: The antigen is sensitive to alpha-N-acetylgalactosaminidase, but not to sialidase or alpha-fucosidase. Various mono- and difucosyl A determinants, either type 1 or type 2 chain, cross-react with both antibodies. The reactivity with both antibodies can be created by treatment of glycophorin A of normal erythrocytes with sialidase followed by beta-galactosidase. N-[3H]acetylgalactosamine can be released by galactose oxidase/NaB3H4 treatment from the Lu65 mucin-like glycoprotein but not from the mucin-like glycoprotein of normal colonic mucosa upon reductive beta-elimination (alkaline borohydride treatment). The antigen may be one of the tumor-associated A cross-reacting antigens occurring in a wide variety of human adenocarcinomas of hosts belonging to all ABO blood groups.
...
PMID:Blood group A cross-reacting epitope defined by monoclonal antibodies NCC-LU-35 and -81 expressed in cancer of blood group O or B individuals: its identification as Tn antigen. 241 56

In this study we further define cell surface carbohydrate structures relevant to cellular interactions that regulate erythropoiesis. An analysis of thymocyte cell surface negativity was made using fluoresceinated poly-L-ornithine (FITC poly-L-ornithine) as a probe that binds to negatively charged sites (i.e., sialic acid residues) at the cell surface. Two distinct subpopulations are labeled, comprising both intensely as well as weakly fluorescent subpopulations of thymocytes. Prior treatment of thymocytes with Vibrio cholerae neuraminidase (VCN), which removes cell surface sialic acid residues, markedly reduced the FITC poly-L-ornithine surface labeling of these cells. Distinct enzymatic modifications of regulatory cell functions were also assessed by the ability of thymocytes to function as separate regulatory subpopulations. Confirming our previous observations, treating thymocytes with VCN impaired the enhancement activity but had little effect on thymocyte regulatory ability to suppress erythroid colony growth. In contrast, treatment of thymocytes with galactose oxidase (GAO) or beta-galactosidase (beta-GAL) removed suppressor activity either before or after VCN treatment. A further exposure of GAO-treated thymocytes to sodium borohydride or hydroxylamine, which reduce D-galactose residues, restores their suppressor function and prevents enhancement. These differential enzymatic effects on thymocyte regulatory cell functions suggest that different carbohydrate structures may be involved in helper and suppressor activities for erythroid colony formation. Sialic acid residues may be associated with certain cells that function to enhance erythropoiesis, and D-galactose residues may be associated with the suppressor subpopulation.
...
PMID:Effects of neuraminidase on the regulation of erythropoiesis: III: Characterization of carbohydrate moieties on the surface of thymic regulatory cells that interact with erythroid colony-forming cells. 256 44


1 2 3 Next >>

---