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:3.1.6.1 (
sulfatase
)
3,205
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Iduronate
sulfatase
of human placenta separates on DEAE Bio-Gel A chromatography into two components, a less acidic form A and a more acidic form B. The two forms have different mobilities on gel electrophoresis and different isoelectric points, pH 5.0 for form A and pH 4.5 for form B. They show the same pH optima in sodium acetate buffer and similar Km values for [3H]disulfated disaccharide substrate. Iduronate
sulfatase
A is more heat labile than iduronate sulfatase B. Different molecular weights were found by gel filtration while similar values were estimated by sucrose gradient centrifugation.
Neuraminidase
treatment of the two forms gives evidence that these enzymes contain sialic acid residues.
...
PMID:Identification and partial characterization of two enzyme forms of iduronate sulfatase from human placenta. 694 76
Despite numerous studies on
arylsulfatase A
, the structure of the glycans present in each of its two subunits has not been determined. This is important because the carbohydrate component of human
arylsulfatase A
synthesized in tumor tissues and transformed cells has been shown to undergo apparent changes. This study elucidates some of their major features. Glycan chain analysis of native and deglycosylated
arylsulfatase A
as well as its subunits was performed with the use of a Glycan Differentiation Kit and lectin affinity chromatography. Each of the two subunits of
arylsulfatase A
from placenta, separated electrophoretically on polyacrylamide gel in reducing conditions, reacted with digoxigenin-labelled Galantus nivalis agglutinin and Aleuria aurantia agglutinin, while those from liver enzyme reacted with the former only. The subunits of both enzymes did not react with Sambucus nigra, Maakia amuriensis, Datura stramonium or Peanut agglutinin. Deglycosylation of
arylsulfatase A
with peptide N-glycosidase F and endo-beta-N-acetylglucosaminidase F resulted in complete cleavage of its carbohydrate component from each subunit. Their molecular weights decreased by 3 kDa.
Neuraminidase
treatment of the enzyme from liver and placenta followed by isoelectrofocusing separation showed the presence of sialylated forms which constituted a small percentage of total enzyme activity. Placental
arylsulfatase A
became bound to Lens culinaris agglutinin agarose, while no interaction with Ricinus communis or Griffonia simplicifolia agglutinin agarose was observed. The study shows that both subunits of
arylsulfatase A
from human placenta possess two high mannose/hybrid type glycans as major structures, with at least one 6-O-L-fucose bound to the innermost N-acetylglucosamine on each.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Characterization of human arylsulfatase A glycans. 789 Jan 20
It has been shown that the concentration of
arylsulfatase A
increases in the body fluids of patients with some forms of cancer and the carbohydrate component of
arylsulfatase A
synthesized in tumor tissues and transformed cells undergoes increased sialylation, phosphorylation and sulfation. The specificity of changes in the glycosylation of glycoproteins in cancer is still unknown. To understand the significance of any changes in glycosylation of
arylsulfatase A
in cancer, it is important to know the structure of its carbohydrate component in normal tissue. Here, carbohydrate moieties of human placental
arylsulfatase A
were studied by sequential lectin affinity chromatography after enzymatic cleavage and labelling with tritiated sodium borohydride. Labelled oligosaccharides were subjected to ion exchange chromatography. The uncharged fraction and the neuraminidase treated charged fraction were further analysed using the lectins: Concanavalin A (Con A), Ricinus communis (RCA I), Triticum vulgaris (L-PHA) and Aleuria aurantia (AAL). The results indicated that 97% of the
arylsulfatase A
oligosaccharides were low molecular weight high mannose type glycans possessing up to 5 mannose residues. This was supported by the approximately 2.4 kDa decrease in the molecular weight of
arylsulfatase
. A subunits upon complete peptide N-glycosidase F deglycosylation, as shown using SDS-PAGE. The remaining 3% of the
arylsulfatase A
oligosaccharides were of the high mannose type, possessing more than 5 mannose residues. Most (97.5%) of the glycans were uncharged, while 2.5% were charged.
Neuraminidase
treatment of the latter did not remove the charge, suggesting the presence of phosphate or sulfate residues. This study, of
arylsulfatase A
oligosaccharides separated from the protein part, shows that all glycans of the enzyme from human placenta are of the high mannose type.
...
PMID:Arylsulfatase A from human placenta possesses only high mannose-type glycans. 920 26
