TY - JOUR
T1 - Multiple molecular forms of α-glucosidase from spinach seeds, spinacia oleracea l.
AU - Sugimoto, Manabu
AU - Furui, Satoshi
AU - Suzuki, Yukio
N1 - Funding Information:
This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan.
PY - 1995/1
Y1 - 1995/1
N2 - Four molecular forms of α-glucosidase were isolated from spinach seeds by several kinds of chromatography. The molecular masses of α-glucosidases I, II, III, and IV were 78, 78, 82, and 82 kDa by SOS–PAGE, and 62, 62, 190, and 70 kDa by gel filtration, respectively. α-Glucosidases I and II showed similar enzymatic properties, in which the Km for soluble starch was about 10 times lower than that for maltose, and they had higher activity not only toward malto-oliosaccharides but also toward α-glucans. The optimum pH was 4.5-5.5 and about 50% of the activity remained after incubation at 70°C for 20 min. On the other hand, α-glucosidases III and IV showed similar enzymatic properties, in which the Km for maltose was 3-4 times lower than that for soluble starch, and they had high activity toward malto-oligosaccharides but faint activity toward α-glucans. The optimum pH was 4.5-5.0 and no activity was found after incubation at 70°C for 20 min. However, anti-α-glucosidase III serum formed precipitation specifically with α-glucosidase III.
AB - Four molecular forms of α-glucosidase were isolated from spinach seeds by several kinds of chromatography. The molecular masses of α-glucosidases I, II, III, and IV were 78, 78, 82, and 82 kDa by SOS–PAGE, and 62, 62, 190, and 70 kDa by gel filtration, respectively. α-Glucosidases I and II showed similar enzymatic properties, in which the Km for soluble starch was about 10 times lower than that for maltose, and they had higher activity not only toward malto-oliosaccharides but also toward α-glucans. The optimum pH was 4.5-5.5 and about 50% of the activity remained after incubation at 70°C for 20 min. On the other hand, α-glucosidases III and IV showed similar enzymatic properties, in which the Km for maltose was 3-4 times lower than that for soluble starch, and they had high activity toward malto-oligosaccharides but faint activity toward α-glucans. The optimum pH was 4.5-5.0 and no activity was found after incubation at 70°C for 20 min. However, anti-α-glucosidase III serum formed precipitation specifically with α-glucosidase III.
UR - http://www.scopus.com/inward/record.url?scp=0028890556&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028890556&partnerID=8YFLogxK
U2 - 10.1080/bbb.59.673
DO - 10.1080/bbb.59.673
M3 - Article
AN - SCOPUS:0028890556
VL - 59
SP - 673
EP - 677
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 4
ER -