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)
Two glycosulfatases [
EC 3.1.6.3
], I and II, were purified 31.3- and 33.9-fold respectively, from a crude extract of the liver of Charonia lampas. The purification was carried out by the following chromatographic procedures; phosphocellulose, Sephadex G-150, Concanavalin A-Sepharose and isoelectric focussing. The enzyme preparations obtained were practically free from
arylsulfatase
[
EC 3.1.6.1
] contamination. Both glycosulfatases are probably glycoproteins differing in their carbohydrate moieties. The molecular weights of
glycosulfatase
I and II were estimated to be about 112,000 and 79,000 respectively. They had the same optimum pH of 5.5, and the same Km value of 25.0 mM for glucose 6-sulfate.
...
PMID:Two glycosulfatases from the liver of a marine gastropod, Charonia lampas. Partial purification and properties. 0 53
Ascorbate-2-sulfate sulfohydrolase was purified 184-fold from a crude extract of the liver of Charonia lampas. In all purification steps including phosphocellulose, first and second Sephadex G-150 column chromatographies, the enzyme activity eluted together with
arylsulfatase
[ED 3.1.6.1] activity, and was separated from
glycosulfatase
]
EC 3.1.6.3
] activity. The nonidentity of ascorbate-2-sulfate sulfohydrolase and
glycosulfatase
was further confirmed by an isoelectric focussing study. Ascorbate-2-sulfate sulfohydrolase had an isoelectric point, pI, of 4.9, and had maximum activity at pH 4.0. Its molecular weight was estimated to be about 154.000.
...
PMID:Copurification of L-ascorbate-2-sulfate sulfohydrolase and arylsulfatase activities from the liver of a marine gastropod, Charonia lampas. 23 88
Sulphatide, cerebroside 3-sulphate was hydrolyzed at a considerable rate by arylsulphatase (aryl-sulphate sulphohydrolase,
EC 3.1.6.1
) purified from a marine gastropod, Charonia lampas. However, it was scarcely hydrolyzed by glycosulphatase (sugar-sulphate sulphohydrolase,
EC 3.1.6.3
) from the same origin. The same was observed with seminolipid, a sulphoglycerogalactolipid. The enzymatic characteristics of both sulphogalactolipid and sulphohydrolase activities of the arylsulphatase were determined as follows. The enzyme activities are stimulated by the addition of sodium taurodeoxycholate and MnCl2. The pH optimum of sulphatide sulphohydrolase activity was pH 5.0, while seminolipid sulphohydrolase activity had maximum activity at pH 5.5. Both of these pH versus activity curves were broad. The Km value was 6.22-10-5 M for both substrates. However, the V values were sulphatide were lower by a factor of one-third than those with seminolipid. These enzyme activities were inhibited by substrates of the arysulphatase, i.e., p-nitrophenyl sulphate, p-nitrocatechol sulphate, ascorbate 2-sulphate and each other sulphogalactolipid, but not by glucose 6-sulphate. Sulphate and phosphate anions inhibited both of the enzyme activities.
...
PMID:Sulphogalactolipid sulphohydrolase activity of arylsulphatase purified from a marine gastropod Charonia lampas. 93 79
