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Two Glycosulfatases from the Liver of a Marine Gastropod , Charonia Lampas

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Two Glycosulfatases from the Liver of a Marine Gastropod , Charonia Lampas J. Biochem., 79, 27-34 (1976) Two Glycosulfatases from the Liver of a Marine Gastropod , Charonia lampas Partial Purification and Properties1 Hiroshi HATANAKA, Yoko OGAWA , and Fujio EGAMI Mitsubishi-Kasei Institute of Life Sciences , Minamiooya, Machida-shi, Tokyo 194 Received for publication , July 9, 1975 Two glycosulfatases [EC 3.1 .6.3], I and ‡U, 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 , S ephadex G-150, Concanavalin A-Sepharose and isoelectric focussing . The enzyme preparations obtained were practically free from arylsulfatase [EC 3.1.6.1] contami nation. Both glycosulfatases are probably glycoproteins differing in their carbohydrate moieties. The molecular weights of glycosulfatase I and H 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 25.0mM for glucose 6-sulfate . As a result of recent investigations on sul yet been fully investigated. Glycosulfatase was fatase reactions, the physiological significance found first in molluscs by Soda and co-workers of arylsulfatase [EC 3. 1. 6. 1] is gradually being (10) and later in microorganisms, but its oc- elucidated. The hydrolysis of naturally oc currence in higher animals is doubtful (11). curring sugar-sulfate derivatives by arylsul In the present investigation, we studied fatase has been reported in the cases of sulfo the partial purification and some properties of galactolipids (1-5), UDP - N- acetylgalacto two glycosulfatases from the liver of a marine samine 4-sulfate (6, 7), and ascorbate 2-sulfate gastropod, Charonia lampas. (8, 9). Each derivative is apparently one of the physiological substrates of arylsulfatase. EXPERIMENTAL In spite of its name, glycosulfatase does not seem to participate in the hydrolysis of these Materials-D-Glucose 6-sulfate (potassium sugar-sulfates, as found in the case of Charonia salt) was purchased from Seikagaku Kogyo. lampas glycosulfatases [EC 3.1.6.3] (5). In p-Nitrophenyl sulfate (potassium salt) obtained any event, the glycosulfatase reaction, includ from Boehringer was recrystallized from 60% ing its enzymological characterization, has not aqueous ethanol. Glucose oxidase [EC 1.1.3.4] and standard proteins for molecular weight 1 This paper is No . ‡Y of the series " Ascorbate-2- estimation were purchased from Boehringer. sulfate Sulfohydrolase." The preceding paper in Concanavalin A was obtained from Sigma. this series is Ref. 5. Eight other lectins were gifts from Prof. T. Vol. 79, No. 1, 1976 27 28 H. HATANAKA, Y. OGAWA, and F. EGAMI Osawa (University of Tokyo). Methyl ƒ¿-D- Enzyme Assays- Glycosulfatase activity glucoside and methyl ƒ¿-D-mannoside were pur was usually assayed by measuring the liberated chased from Merck. Ascorbate 2-sulfate sulfate according to the method previously de (potassium salt) was synthesized by the method scribed (8). For particular purposes, the described previously (8, 12). amount of liberated glucose was measured by Other chemicals were of reagent grade. the use of glucose oxidase. Instead of termi Preparation of Glycosulfatases I and ‡U nation by the addition of 0.4ml of 0.15N HCl For the preparation of crude extract, the liver and 0.4ml of barium chloride-gelatin solution (hepatopancreas) (100g) of C. lam pas was (14), the reaction was terminated by putting homogenized as described previously (8). The the container in ice-water and adding 0.1ml dialyzed 105,000•~g supernatant was applied of 0.2M sodium-potassium phosphate buffer, to a phosphocellulose (Brown) column (2.65•~43 pH 5.8. An aliquot of the mixture was added cm, 237ml) equilibrated with 0.01M sodium to the preconditioned glucose oxidase reaction acetate-acetic acid buffer, pH 5.0. The frac mixture, in a final volume of 3ml, containing tions of the main peak containing both glyco 2ml of 0.2M sodium-potassium phosphate sulfatase and arylsulfatase activities which buffer, pH 5.8, and 0.1mg of glucose oxidase eluted at 0.2M sodium chloride were pooled. protein (of fungal origin ; Boehringer grade I, These fractions were concentrated using an approx. 210U/mg). The rate of oxygen con Amicon model 402 pressure-filtration cell with sumption during the oxidation of glucose was a PM-10 membrane. The sample was applied measured with an oxygen probe (Yellow Spring to a Sephadex G-150 (Pharmacia) column (2.1•~ Inst., type YSI 5331). The reaction was car 132cm, 454ml). The fractions which eluted ried out at 37? with constant stirring. just behind the void peak contained most of Arylsulfatase activity was measured by the the glycosulfatase and arylsulfatase activities, method described in previous papers (8, 15). forming partially overlapping peaks. They Molecular Weight Estimation-The method were collected together. of Andrews (16) was followed for the estima Concanavalin A-Sepharose (Pharmacia) col tion of the molecular weight of glycosulfatases umn chromatography was used for the separa I and ‡U by gel filtration. A column of Sepha tion of the two glycosulfatases. The gel was dex G-200 (1.25•~48cm, 58.9ml) eluted with equilibrated with 0.02 M sodium acetate-acetic 0.05M Tris-HC1 buffer, pH 7 .5, containing 0.1 acid buffer, pH 5.5, containing 0.5M sodium M potassium chloride was used. The follow chloride, 0.5mM MnC12, and 0.5 mM CaC12, ing standards were utilized : horse heart cyto and packed in a small column (1.25•~8.5cm, chrome c, bovine serum albumin , yeast glucose- 10.4ml). The sample was adjusted to 0.5M 6 - phosphate dehydrogenase [EC 1. 1. 1. 49] , sodium chloride, 0.5mM MnC12, and 0.5mM rabbit muscle aldolase [EC 4 .1.2.13], beef liver CaC12, and applied at a flow rate of 3.0ml/hr. catalase [EC 1.11.1.6], and beef liver glutamate Fractions of 2ml were collected. Elution was dehydrogenase [EC 1.4 .1.3]. done with the same buffer containing 0.5M Precipitation of Glycosulfatases I and II methyl ƒ¿-D-glucoside and 0.1M methyl ƒ¿-D with Various Lectins - The precipitation of mannoside. glycosulfatases with various lectins was carried For the separation of glycosulfatase ‡U and out at 4? in a screw-capped polycarbonate tube arylsulfatase retained together on the Con (1.6•~7.6cm) using the following mixture ; 0.14 canavalin A-Sepharose gel, isoelectric focussing M Tris-acetic acid buffer , pH 7.5, 11mM CaC12, was done with an LKB model 8100 Ampholine 11mM MnC12, 0.11M sodium chloride , about unit. The ampholyte, isoelectric between pH 0.5mg/ml each of nine species of lectins , and 3.0 to 7.0, was used in a total volume of 110 16.1ƒÊg of protein/ml of glycosulfatase I or 10 .9ƒÊ Ml. g of protein/ml of glycosulfatase ‡U. The final Determination of Protein-The method of volume was 0.5ml in each case . After 1 day, Lowry et al. (13) was used routinely with bo the mixture was centrifuged at 105 ,000•~g for vine serum albumin as a standard. 60min using a Spinco type 50 Ti rotor . An J. Biochem. C. lampas GLYCOSULFATASES 29 aliquot of the resulting supernatant was used graphic profile. The passed-through fractions for the determination of glycosulfatase activ contained about half of the glycosulfatase ac ity. The remainder of the supernatant and tivity, but no arylsulfatase activity. Arylsul precipitate were mixed again. These suspen fatase activity together with the rest of the sions were kept standing at 4? for 2 days more, glycosulfatase activity was retained on the -and were then centrifuged in the same man Concanavalin A-Sepharose gel. This result ner. The enzyme activity in the supernatant suggests that the two retained enzymes, i.e., was measured. arylsulfatase and half of the glycosulfatase, namely glycosulfatase ‡U, may be glycoproteins. RESULTS The passed-through glycosulfatase, name ly glycosulfatase I, was subjected to a second Partial Purification of Glycosulfatases I Concanavalin A-Sepharose column chromatog and ‡U-After the phosphocellulose and Sepha raphy, in order to minimize arylsulfatase con dex G-150 column chromatographies, the sam tamination. The purification procedures for ple was applied to a Concanavalin A-Sepharose glycosulfatase I are summerized in Table I. column. Figure 1 represents the chromato- Fig. 1. Concanavalin A-Sepharase column chroma tography of the eluate from the Sephadex G-150 column. The broken line with filled circles repre sents the absorbance at 280nm. Enzyme activities of glycosulfatase and arylsulfatase, represented as solid lines with open triangles and open circles, respectively, were determined as follows: The assay mixture for glycosulfatase, in a total volume of 200 pl, contained 5ƒÊmoles of D-glucose 6-sulfate, 20ƒÊmoles of sodium acetate-acetic acid buffer, pH 5.7, and the enzyme. After reaction for 60 min at 37?, the resulting turbidity produced by adding barium chloride-gelatin solution was measured at 360nm. The assay mixture for arylsulfatase, in a total volume of 300ƒÊl, contained 3ƒÊmoles of p- nitrophenyl sulfate, 30ƒÊmoles of Tris-acetic acid buffer, pH 7.5, and the enzyme. The reaction was carried out at 37? in a Gilford model 2400-2 Tecord ing spectrophotometer. One unit of each enzyme represents 1ƒÊmole/min. TABLE I. Purification of glycosulfatase I from the liver of C. lampas. Vol. 79, No. 1, 1976 30 H. HATANAKA, Y. OGAWA, and F. EGAMI Glycosulfatase I was purified 31.3 fold, and glycosulfatase I seemed to be attributable to was practically free from arylsulfatase. As p - nitrophenyl sulfate- hydrolyzing activity, mentioned below (shown in Fig. 3), the very which had an optimum pH of 5.0. small activity of arylsulfatase, measured at pH The glycosulfatase ‡U retained on the Con 7.5, contained in the purified preparation of canavalin A-Sepharose gel was subjected to isoelectric focussing to separate it from aryl sulfatase, as shown in Fig.
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