Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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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

Two monoclonal antibodies, HH8 and HH9, have been established after immunization of mice with galactosyl-A glycolipid antigen having the terminal structure, Gal beta 1----3GalNAc alpha 1----3[Fuc alpha 1----2]Gal beta 1----R, which is the precursor for type 3 chain A (repetitive A) and type 3 chain H (A-associated H). Both antibodies react strongly and specifically with galactosyl-A, but HH8 (IgM) showed strong hemagglutination of blood group A1, A2, O and B erythrocytes after sialidase treatment, while HH9 (IgG1) did not react with human erythrocytes even after sialidase treatment. HH8 and anti-T antibody, but not HH9, reacted with glycophorin A after sialidase treatment. The reactivity of HH8 with glycophorin A was abolished by beta-galactosidase and was inhibited by liposomes containing galactosyl-A, but not other glycolipids. In addition, anti-T antibody and peanut lectin reacted specifically with galactosyl-A glycolipids. These findings indicate that HH8 recognizes the terminal disaccharide Gal beta 1----3GalNAc alpha 1----R, which is the same sequence as the classically known Thomsen-Friedenreich antigen (T-antigen), whereas HH9 does not cross-react with T-antigen but recognizes the entire galactosyl-A structure. The T-antigen was also demonstrated by immunohistology with HH8 after neuraminidase treatment in a subset of cells in stratified epithelium.
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PMID:Monoclonal antibodies directed to the blood group A associated structure, galactosyl-A: specificity and relation to the Thomsen-Friedenreich antigen. 328 40

Tryptic glycopeptide T1 of human glycophorin A [Tomita, M., & Marchesi, V. T. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 2964-2968] was subjected to hydrazinolysis. After N-acetylation, the complex-type oligosaccharides were isolated by gel filtration. The major neutral oligosaccharide (2000 molecular weight) was purified by a combination of ion-exchange and gel-permeation chromatography. Treatments with endo- and exo-glycosidases, periodate oxidation, and methylation analysis indicated that the major neutral oligosaccharide has the following structure: Gal beta 1 leads to -4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(GlcNAc beta 1 leads to 4)(Gal beta 1 leads to -4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3)Man beta 1 leads to 4GlcNAc beta 1 leads to 4-(Fuc alpha 1 leads to 6)GlcNAc. This oligosaccharide was retained by Ricinus communis agglutinin-Sepharose and retarded by Sepharose 4B coupled with erythroagglutinating E4 isolectin from Phaseolus vulgaris. Retention by concanavalin A-Sepharose was observed only after treatment of the oligosaccharide with beta-galactosidase.
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PMID:Structure of a complex-type sugar chain of human glycophorin A. 721 94

Whereas a variety of two-hybrid systems are available to measure the interaction of soluble proteins, related methods are significantly less developed for the measurement of membrane protein interactions. Here we present a two-hybrid system to follow the heterodimerization of membrane proteins in the Escherichia coli inner membrane. The method is based on the repression of a reporter gene activity by two LexA DNA binding domains with different DNA binding specificities. When coupled to transmembrane domains, heterodimeric association is reported by repression of beta-galactosidase synthesis. The LexA-transmembrane chimeric proteins were found to correctly insert into the membrane, and reproducible signals were obtained measuring the homodimerization as well as heterodimerization of wild-type and mutant glycophorin A transmembrane helices. The GALLEX data were compared with data recently gained by other methods and discussed in the general context of heteroassociation of single TM helices. Additionally, the formation of heterodimers between the TM domains of the alpha(4) and the beta(7) integrin subunits were tested. The results show that both homo- and heterodimerization of membrane proteins can be measured accurately using the GALLEX system.
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PMID:GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane. 1244 30