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J. Biochem, 1986, Vol. 99, No. 3 693-701
© 1986 Japanese Biochemical Society

other

Purification and Characterization of Two Components of Acid {alpha}-Glucosidase from Pig Liver1

Ken-ichiro TASHIRO*, Teruo IWAMASA**, Hisao KATO***, Shigenori OGATA**** and Motoaki ANAI*,2

*Department of Medical Technology, School of Health Sciences, Kyushu University Higashi-ku, Fukuoka, Fukuoka 812
**Department of Pathology, Ryukyu University School of Medicine Okinawa 903-01
***Department of Biology, Faculty of Science, Kyushu University Higashi-ku, Fukuoka, Fukuoka 812
****Department of Biochemistry, Fukuoka University School of Medicine Nishi-ku, Fukuoka, Fukuoka 814-01

2 To whom reprint requests should be addressed

Acid {alpha}-glucosidase [EC 3.2.1.3 [EC] ] was purified from pig liver by a procedure including Sephadex G-100 affinity chromatography. Electrophoresis on SDS-polyacrylamide gel of the purified enzyme indicated the presence of two components with molecular weights of 73K and 64K. The two components of the enzyme were completely separated, in reasonable yield, by chromatography on a DEAE-5PW column. Both components catalyzed the hydrolysis of the {alpha}-1,4 and {alpha}-1,6 linkages of glycogen, maltose, isomaltose, dextrin, and a synthetic glucoside at acid pH. The pH optima of both components were 4.3 for maltase and glucoamylase, and 4.8 for isomaltase and dextrinase. But as to the activity on 4MU-{alpha}-Glc, the pH optimum of the larger component was 4.8 and that of the smaller component 5.3. The Km values of both components for 4MU-{alpha}-Glc, maltose, glycogen, isomaltose, and dextrin were 1.0×10–4 M, 9.1×10–3 M, 16.7 mg/ml, 6.7×10–2 M, and 12.5 mg/ml, respectively. Erythritol, Tris, and turanose inhibited the two components competitively. The Kl values of the larger component were 5.0×10–2 M, 13.3×10–3 M, and 3.2×10–3 M, and those of the smaller component were 2.5×10–2 M, 6.1×10–3 M, and 4.7×10–3 M, for erythritol, Tris, and turanose, respectively.

1 This investigation was supported in part by a grant from the Jishiro Nakamura Memorial Fund.


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