Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Highly sensitive technique are described for the assay of plasma membrane (5'-nucleotidase, alkaline phosphatase), microsomal (neutral alpha-glucosidase, leucyl-2-naphthylamidase) and biliary canalicular (gamma-glutamyltransferase) enzymes and for nine acid hydrolases (acid phosphatase, phosphodiesterase, beta-glucosidase, alpha-glucosidase, alpha-galactosidase, beta-galactosidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, beta-glucuronidase) in human liver. 2. Optimum and specific assay systems have been developed which give linear kinetics for all enzymes. 3. The range of enzyme activities in samples of human liver, obtained by closed needle biopsy, and sera have been determined.
Clin Sci Mol Med 1977 Mar
PMID:Enzyme activities in human liver biopsies: assay methods and activities of some lysosomal and membrane-bound enzymes in control tissue and serum. 1 4

This is a review of the properties and molecular genetics of six lysosomal hydrolases: beta-galactosidase, hexosaminidases A and B, alpha-galactosidase, beta-glucosidase and alpha-fucosidase. Each enzyme is discussed with regards to isoenzymes and substrate specificity, subunit structure, genetic relationship of isoenzymes and genetic variants. The molecular genetics of human diseases caused by deficiencies of each enzyme are discussed.
Mol Cell Biochem 1977 Oct 07
PMID:Glycosphingolipid hydrolases: properties and molecular genetics. 20 Aug 37

The two mutants (abs) and (wal) affecting the cell morphology of yeast lead also to higher in vivo activities of the cell wall enzymes acid phosphatase, invertase and melibiase.
Mol Gen Genet 1979 Jun 07
PMID:Pieiotropic effect of two cell wall mutants on the activity of some cell wall enzymes in the yeast Saccharomyces cerevisiae. 22 35

An enzyme with alpha-galactosidase activity and an apparent molecular weight of 82 kDa was purified from culture medium of Aspergillus niger. The N-terminal amino acid sequence of the purified protein shows similarity to the N-terminal amino acid sequence of alpha-galactosidases from several other organisms. Oligonucleotides, based on the N-terminal amino acid sequence, were used as probes to clone the corresponding gene from a lambda EMBL3 gene library of A. niger. The cloned gene (aglA) was shown to be functional by demonstrating that the 82 kDa alpha-galactosidase is absent from a strain with a disruption of the aglA gene, and is over-produced in strains containing multiple copies of the aglA gene. Enzyme activity assays revealed that the 82 kDa alpha-galactosidase A represents a minor extracellular alpha-galactosidase activity in A. niger.
Mol Gen Genet 1992 Jun
PMID:Cloning and expression of a member of the Aspergillus niger gene family encoding alpha-galactosidase. 132 Jan 86

F62 LOS of Neisseria gonorrhoeae consists of two components. The higher molecular weight (MW) component is recognized by monoclonal antibody (MAb) 1-1-M and the smaller MW component by MAb 3F11. Epitope expression of the two LOS components and their partial structures were investigated by treating the F62 LOS with several glycosidases and then monitoring their antigenicity with the two mouse IgM MAbs. The 1-1-M-defined LOS component was cleaved with both beta-N-acetylhexosaminidase and endo-beta-galactosidase, and each cleavage resulted in the loss of expression of the 1-1-M-defined epitope. The N-acetylhexosamine (HexNAc) released by the hexosaminidase was found to be GalNAc, and the smaller oligosaccharide released by the endo enzyme was identified to be a dimer GalNAc beta----Gal. In contrast, the MAb 3F11-defined LOS component was not digested by the endo galactosidase, but it was cleaved with alpha and beta-galactosidase, and expression of the MAb 3F11-defined LOS epitope expression of the MAb 3F11-defined LOS was abolished by the treatment with each of two exo enzymes. MAb 3F11 bound to the 1-1-M-defined LOS component resulting from the removal of the beta-GalNAc residue, and the resulting LOS was further cleaved with beta-galactosidase, but not with alpha-galactosidase. From these results, we conclude the following: (1) MAbs 1-1-M and 3F11 both recognize the non-reducing termini of the LOS components; (2) the 1-1-M-defined LOS component has the GalNAc beta----Gal beta 1----4-Glc (or GlcNAc) structure, and the GalNAc beta----Gal residue is involved in the MAb 1-1-M-defined epitope; (3) the MAb 3F11-defined LOS component may not have a Gal beta 1----4GlcNAc beta 1----4Gal beta 1----4Glc structure within the molecule. However, it has beta-Gal residue at its non-reducing terminus, and this residue is involved in the MAb 3F11-defined epitope; (4) the two LOS components share a similar antigenic structure, and the 3F11-defined epitope structure is present in the MAb 1-1-M-defined LOS component. Expression of this epitope within the 1-1-M-defined LOS molecule is blocked by the beta-GalNAc residue; however, the beta-GalNAc residue at the non-reducing end may be not the only structural difference between the two components.
Mol Immunol 1991 Nov
PMID:Epitope expression and partial structural characterization of F62 lipooligosaccharide (LOS) of Neisseria gonorrhoeae: IgM monoclonal antibodies (3F11 and 1-1-M) recognize non-reducing termini of the LOS components. 172 May 5

The ability of industrial strains of mesophylic Streptococcus diacetylactis to synthesize the enzyme beta-galactosidase has been studied. Among the 22 studied strains 8 were found to synthesize the enzyme. Plasmid DNA was isolated from the Streptococcus diacetylactis strain 144 possessing the highest level of beta-galactosidase activity. The cells of the strain harbour the 35, 40 and 60 kb plasmids. The alpha-galactosidase genes from this strain was cloned in Escherichia coli cells. The gene is located on the BglIII DNA fragment of the total plasmid DNA from Streptococcus diacetylactis the size of 2.8 kb. Following the Sau3A restriction endonuclease digestion the gene was subcloned on a birepliconed vector plasmid pCB20. The latter is capable of replication in the Gram-negative as well as Gram-positive microorganisms. The pCB20 derivatives carrying the different length fragments with the beta-galactosidase gene were isolated. DNA of an obtained plasmid was used for transformation of Streptococcus diacetylactis cells. The presence of the recombinant plasmid in streptococcus strain 144 results in the 1.8 fold increase in beta-galactosidase production.
Mol Gen Mikrobiol Virusol 1991 Jun
PMID:[Structure of the beta-galactosidase gene from Streptococcus diacetylactis 144 and its expression in Escherichia coli and Streptococcus diacetylactis cells]. 194 24

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.
Mol Biochem Parasitol 1990 Feb
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

Polyadenylated mRNA was purified from the aleurone cells of Cyamopsis tetragonoloba (guar) seeds germinated for 18 h and used for the construction of a cDNA library. Clones with the alpha-galactosidase encoding gene were identified using oligo-nucleotide mixed probes based on the NH2 terminal amino acid sequence and on the sequence of an internal peptide. The nucleotide sequence of the cDNA clone showed that the enzyme is synthesized as a precursor with a 47 amino acid NH2 terminal extension. This pre-sequence most likely functions to target the protein outside the aleurone cells into the endosperm. Based upon structural features, it is proposed to divide the precursor into a pre-(signal sequence) part and a glycosylated pro-part comparable with those of the yeast mat A/alpha factor and killer factor. A comparison of the derived amino acid sequence of this alpha-galactosidase from plant origin revealed significant stretches of homology with respect to the amino acid sequences of the enzymes from Saccharomyces cerevisiae and from human origin but only to a minor extent compared with the alpha-galactosidase from Escherichia coli.
Plant Mol Biol 1989 Nov
PMID:Cloning and nucleotide sequence of the alpha-galactosidase cDNA from Cyamopsis tetragonoloba (guar). 257 96

Part of the higher-order structure of chromatin is achieved by constraining DNA in loops ranging in size from 30 to 100 kilobase pairs; these loops have been implicated in defining functional domains and replicons and possibly in facilitating transcription. Because the human active and inactive X chromosomes differ in transcriptional activity and replication, we looked for differences in their chromatin loop structures. Since the islands of CpG-rich DNA at the 5' ends of X-linked housekeeping genes are the regions where functional differences in DNA methylation and nuclease sensitivity are found, we looked for scaffold association of these sequences after extraction of histones with lithium diiodosalicylate. Specifically, we examined the 5' CpG islands within the hypoxanthine phosphoribosyltransferase, glucose 6-phosphate dehydrogenase, P3, GdX, phosphoglycerate kinase type 1, and alpha-galactosidase loci in human lymphoblasts obtained from individuals with 1 to 4 X chromosomes. Although we detected no scaffold-associated regions near these genes, we found several such regions at the ornithine transcarbamylase and blood clotting factor IX loci. Our results suggest that the CpG islands are excluded from the nuclear scaffold and that even though transcriptionally active, housekeeping genes are less likely than X-linked tissue-specific genes to be scaffold associated. In all cases, the pattern of scaffold association was the same for loci on active and inactive X chromosomes.
Mol Cell Biol 1989 Jun
PMID:Chromatin loop structure of the human X chromosome: relevance to X inactivation and CpG clusters. 276 35

The presence of terminal alpha-D-galactosyl residues in the carbohydrate chains of glycoprotein antigens from the asexual blood stages of Plasmodium falciparum is demonstrated by the alpha-D-galactosidase sensitivity of particular parasite antigens, the use of specific glycosidases to cleave sugars from parasite glycoproteins radiolabeled with [3H]glucosamine, and the ability of Bandeirea simplicifolia lectin, which has a specificity for terminal alpha-galactosyl residues, to bind to the parasite. The carbohydrate side chains, and in particular the terminal alpha-galactosyl residues, are shown to have an important role in determining the binding of antibodies to parasite glycoproteins.
Mol Biochem Parasitol 1986 May
PMID:Terminal galactose residues and the antigenicity of Plasmodium falciparum glycoproteins. 301 31


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