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Sulfatide and Seminolipid As Substrates of Charonia Lampas Arylsulfatasel

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Sulfatide and Seminolipid As Substrates of Charonia Lampas Arylsulfatasel PRELIMINARY COMMUNICATION J . Biochem., 78, 427-429 (1975) Sulfatide and Seminolipid as Substrates of Charonia lampas Arylsulfatasel Hiroshi HATANAKA,* Yoko OGAWA ,* Fujio EGAMI,* Ineo ISHIZUKA,** and Yoshitaka NAGAI** *Mitsubishi-Kasei Institute of Life Sciences , Minamiooya, Machida-shi, Tokyo 194, and **Department of Biochemistry, Tokyo Metropolitan Institute of Gerontology, Itabashi-ku, Tokyo 173 Received for publication, May 15, 1975 The activities of arylsulfatase [EC 3. 1. 6. 1] and glycosulfatase [EC 3. 1. 6. 3] from the liver of Charonia lampas were almost completely separated from each other. Sulfate ester bonds at position 3 of the galactose moiety of sulfatide and seminolipid were easily hydrolyzed by arylsulfatase, but scarcely affected by glycosulfatase. Mammalian arylsulfatase A [EC 3.1. 6. 1] is Charonia lampas, which is known to have known to show sulfatide sulfohydrolase [EC high glycosulfatase and arylsulfatase activities 3.1.6.8] activity (2, 3). In addition, the (9, 10). testicular sulfoglycerogalactolipid, seminolipid, As shown in this paper, both sulfatide was recently reported to be hydrolyzed by and seminolipid were easily hydrolyzed by the the same enzyme (4, 5). This seems rather arylsulfatase from the liver of C. lampas, but remarkable, because the sulfate group of this were scarcely affected by the glycosulfatase lipid is attached to the C-3 hydroxyl group of [EC 3.1.6.3]. the galactose moiety (6, 7). On the other Three species of sulfatases were separated hand, no studies have been made on whether from the liver of C. lampas, glycosulfatase I these sulfogalactolipids can be hydrolyzed by and II, and arylsulfatase. Details of the glycosulfatase, which is known to hydrolyze methods of purification and characterization the sulfate ester linkage at position 6 of of the enzymes will be reported elsewhere.' glucose (8). This is probably because the Arylsulfatase was purified essentially as occurrence of glycosulfatase in higher animals described in a previous paper (11), and was is still doubtful (8). To examine this problem further separated from glycosulfatase by the present experiments were undertaken electrofocussing. Glycosulfatase I and II were with enzyme preparations from the liver separated from each other using a column of (hepatopancreas) of the marine gastropod, Concananavalin A-Sepharose, on which only the latter was retained. 1 This paper is No . V of the series " Ascorbate-2- 2 H sulfate Sulfohydrolase." The preceding paper in this . Hatanaka, Y. Ogawa, and F. Egami, manuscript series is Ref. 1. in preparation. Vol. 78, No. 2, 1975 427 428 PRELIMINARY COMMUNICATION [35S]Sulfatide and [35S]seminolipid were graphy after separation by thin layer chroma prepared from lipid extracts of the brains of tography on silica gel (5). 3-week old rats, 24 hr after intraperitoneal Sulfatide and seminolipid sulfohydrolase injection of [35S]sulfuric acid, as previously activities were measured essentially as de- described (7). Sulfogalactolipids were purified scribed by Porter et al. (12 ). Ascorbate-2- by successive column chromatographies on sulfate sulfohydrolase, arylsulfatase, and Florisil and DEAE-Sephadex A-25 as will be glycosulfatase activities were measured as reported elsewhere, and were proved to be described previously (11, 13). homogeneous by radioscanning or radioauto- Figure 1 shows the pH-activity profiles of the three purified enzymes, glycosulfatase I and II, and arylsulfatase with p-nitrophenyl sulfate and glucose 6-sulfate as substrates. The glycosulfatase I and II preparations showed weak activities with p-nitrophenyl Fig. 1. pH-Activity curves of the three sulfatases from C. lampas liver with p-nitrophenyl sulfate and glucose 6-sulfate as substrates. With p-nitrophenyl sulfate (broken line) as substrate, the assay mixture in a total volume of 300 pl, contained 3 nmoles of p-nitrophenyl sulfate, 30 pmoles of buffer, and en zyme. With glucose 6-sulfate (solid line) as sub strate, the mixture in a total volume of 200 pl, con tained 5 pmoles of glucose 6-sulfate, 20 pmoles of buffer, and enzyme. Enzyme activities were meas ured in sodium acetateacetic acid buffer (filled circles, pH 4.0-5.5), Tris-acetic acid buffer (half-filled circles, pH 6.0-7.5), and Tris-HC1 buffer (open circles, pH 7.5-9.0). The enzyme preparations used were glyco sulfatase I (a), glycosulfatase II (b), and arylsulfatase (c). One unit of enzyme activity represents one micromole of substrate hydrolyzed per min. TABLE I. Activities of the three sulfatases from C. lampas liver on the sulfate esters, ascorbate 2-sulfate, sulfatide, and seminolipid. For ascorbate 2-sulfate, the assay mixture in a total volume of 300 pl, contained 3 pmoles of ascorbate 2-sulfate, 30 ƒÊmoles,of sodium acetate-acetic acid buffer, pH 4.0, 30.nmoles of 2,6- dichlorindophenol, and enzyme. For sulfatide, the mixture in a total volume of 200 pl, contained 18 nmoles of rat brain [35S]sulfatide (379 dpm/nmole), 4 pmoles of MnCl2, 250 leg of sodium taurodeoxycholate, 24 ƒÊmoles of sodium acetate-acetic acid buffer, pH 5.0 and enzyme. For seminolipid the mixture in a total volume of 200 pl, contained 19 nmoles of rat testicular [35S]seminolipid (341 dpm/nmole), 4 pmoles of MnC12 i 250 leg of sodium taurodeoxycholate, 24 ƒÊmoles of sodium acetate-acetic acid buffer, pH 5.5, and enzyme. One unit of activity represents one micromole of substrate hydrolyzed per min. a Activity less than 5•~10-4 unit/mg protein. J. Biochem. HYDROLYSIS OF SULFATIDE BY C. lampas ARYLSULFATASE 429 sulfate with optima at pH 5.0 (Fig. 1-a, b). ascorbate 2-sulfate, and that glycosulfatase is These activities are probably not due to inactive on such natural sugar sulfates in contamination with arylsulfatase because it spite of its name. The results also show that has a pH optimum of 7.5, as shown in Fig. the nomenclature of sulfatases must be revised 1-c. In a separate experiment, the arylsul- and that further studies are required on their fatase preparation showed slight activity with substrate specificities using various sugar glucose 6-sulfate at pH 5.5 (specific activity, sulfate esters. 0.032 units per mg protein.) It is uncertain whether this is due to contamination with REFERENCES glycosulfatase or to very weak activity of 1. Hatanaka, H., Ogawa, Y., & Egami, F. (1975) arylsulfatase against glucose 6-sulfate. J. Biochem. 77, 807-810 The arylsulfatase preparation hydrolyzed 2. Mehl, E. & Jatzkewitz, H. (1968) Biochim. Bio both brain sulfatide and testicular seminolipid, phys. Acta 151, 619-627 as shown in Table I, whereas the glycosulfatase 3. Jerfy, A. & Roy, A.B. (1973) Biochim. Biophys. I and II preparations scarcely hydrolyzed these Acta 293, 178-190 sulfolipids. These results show that sulfatide 4. Yamato, K., Handa, S., & Yamakawa, T. (1974) and seminolipid were hydrolyzed by arylsul J. Biochem. 75, 1241-1247 fatase from the liver of C. lampas, irrespective 5. Fluharty, A.L., Stevens, R.L., Miller, R.T., & of the presence of a large amount of glyco Kihara, H. (1974) Biochem. Biophys. Res. Commun. sulfatase. As in the case of mammalian aryl 61, 348-354 sulfatase A (2-5), taurodeoxycholate and 6. Yamakawa, T., Kiso, N., Handa, S., Makita, A., & Yokoyama, S. (1962) J. Biochem. 52, 226-228 MnCl2 were required for the reaction. The 7. Ishizuka, I., Suzuki, M., & Yamakawa, T. (1973) preparation had pH-optima of 5.0 and 5.5 with sulfatide and seminolipid, respectively, J. Biochem. 73, 77-87 8. Roy, A.B. (1971) in The Enzymes (Boyer, P.D., and these are different somewhat from the ed.) Vol. 5, pp. 1-19, Academic Press, New York value of pH 4.5 of mammalian arylsulfatase. 9. Takahashi, N. & Egami, F. (1961) Biochem. J. It has been suggested that ascorbate 2- 80, 384-386 sulfate, the sulfate ester of a sugar derivative, 10. Nishida-Fukuda, M. & Egami, F. (1970) Biochem. may be hydrolyzed by C. lampas arylsulfatase J. 119, 39-47 (11). This was confirmed in the present 11. Hatanaka, H., Ogawa, Y., & Egami, F. (1975) work (Table I). J. Biochem. 77, 353-359 Artificial substrates, such as p-nitro 12. Porter, M.T., Fluharty, A.L., De La Flor, S.D., catechol sulfate and p-nitrophenyl sulfate are & Kihara, H. (1972) Biochim. Biophys. Acta 258, 769-778 most frequently used for in studies on aryl 13. Hatanaka, H., Ogawa, Y., & Egami, F. (1974) sulfatase. So the physiological significance of J. Biochem. 75, 861-866 arylsulfatase is uncertain (14 ). The present 14. Nicholls, R.G. & Roy, A.B. (1971) in The En work indicates that arylsulfatase hydrolyzes zymes (Boyer, P.D., ed.) Vol.5, pp.21-41, Aca various natural sulfate esters of sugar demic Press, New York derivatives, such as sulfatide, seminolipid, and Vol. 78, No. 2, 1975.
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