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Results for “SULFATASES”

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At least 775 records · Page 43Linked to original sources
PubMed2006

Enzyme replacement therapy for mucopolysaccharidosis VI: a phase 3, randomized, double-blind, placebo-controlled, multinational study of recombinant human N-acetylgalactosamine 4-sulfatase (recombinant human arylsulfatase B or rhASB) and follow-on, open-label extension study.

OBJECTIVE: The objective of this Phase 3 study was to confirm the efficacy and safety of recombinant human arylsulfatase B (rhASB) treatment of mucopolysaccharidosis type VI (MPS VI; Maroteaux-Lamy syndrome), a rare, fatal lysosomal storage disease with no effective treatment. STUDY DESIGN: Thirty-nine patients with MPS VI were evaluated in a randomized, double-blind, placebo-controlled, multicenter, multinational study for 24 weeks. The primary efficacy variable was the distance walked in a 12-minute walk test (12MWT), whereas the secondary efficacy variables were the number of stairs climbed in a 3-minute stair climb (3MSC) and the level of urinary glycosaminoglycan (GAG) excretion. All patients received drug in an open-label extension period for an additional 24 weeks. RESULTS: After 24 weeks, patients receiving rhASB walked on average 92 meters (m) more in the 12MWT (p=.025) and 5.7 stairs per minute more 3MSC (p=.053) than patients receiving placebo. Continued improvement was observed during the extension study. Urinary GAG declined by -227+/-18 microg/mg more with rhASB than placebo (p<.001). Infusions were generally safe and well tolerated. Patients exposed to drug experienced positive clinical benefit despite the presence of antibody to the protein. CONCLUSION: rhASB significantly improves endurance, reduces GAG, and has an acceptable safety profile.

Adolescent↗
PubMed1976

Aryl sulfatase activity in mouse molar odontogenesis.

Arylsulfatase activity has been studied in the developing molar of the Swiss albino mouse from the lamina stage to the appositional stage. Timed-pregnant Swiss albino mice were utilized in this study. Females were sacrificed by ether anesthesia and fetuses extirpated or newborns anesthetized and decapitated. Frozen sections were fixed and incubated for arylsulfatase activity according to a modification of the method of PEARSE (1972). The tissue was dehydrated, cleared and covered. Phase light microscopy was utilized in evaluating arylsulfatase activity in the developing molar. Arylsulfatase activity was evaluated for each stage of development and the results presented in tabular form. The present investigation represents the first known effort to describe arylsulfatase activity in odontogenic tissues from the initiation of the dental lamina through the appositional stage. Arylsulfatase activity appeared to be related to the degree of vascularization of the developing enamel organ and adnexa and the beginning of hard tissue elaboration.

Animals↗
PubMed1997

Improved high-performance liquid chromatographic method for N-acetylgalactosamine-4-sulfate sulfatase (arylsulfatase B) activity determination using uridine diphospho-N-acetylgalactosamine-4-sulfate.

UDP-N-acetylgalactosamine-4-sulfate (UDP-GalNAc-4-S) was isolated from hen oviduct (isthmus) with a yield of 31 mumol per 100 g of wet tissue and used for arylsulfatase B (ASB) activity determination. Two HPLC methods of separation and quantitation of the reaction product were described: (1) an original gradient elution method which makes it possible to determine the reaction product when only partially purified ASB was used and additional uridine derivatives were formed during incubation; (2) an improved, fast isocratic elution method which may be used in the case of purified ASB preparations, devoid of other nucleotide hydrolysing enzymes. For both methods the detection limit was 0.1 nmol of product with standard error of determination < or = 3%. Using the gradient elution method we have found that UDP-GalNAc-4-S was hydrolysed by bovine arylsulfatase B1 most efficiently at pH 5.0 and concentration 0.5 mM with K(m) = 85 microM.

Animals↗
PubMed2004

Highly enantioselective sec-alkyl sulfatase activity of Sulfolobus acidocaldarius DSM 639.

[reaction: see text] rac-sec-Alkyl sulfate esters 1a-4a were resolved in high enantioselectivities with E-values up to >200 using whole cells of aerobically grown Sulfolobus acidocaldarius DSM 639. The stereochemical course of this biohydrolysis was shown to proceed with strict inversion of configuration; thus, the preferred (R)-enantiomers were converted into the corresponding (S)-sec-alcohols to furnish a homochiral product mixture.

Enzyme Activation↗