ライフサイエンスコーパス: isomaltase

1 its of both maltase-glucoamylase and sucrase-isomaltase.

2 changes in alkaline phosphatase and sucrase isomaltase.

3 Induction of ITF and sucrase-isomaltase after MEK inhibition in HT29-N2 cells did not

4 idases, alpha-glucosidase, beta-glucosidase, isomaltase, alpha-mannosidase, and glucoamylase, were ob

5 ein showed strong homology to rabbit sucrase-isomaltase, an abundant intestinal enzyme.

6 essing high levels of Cdx2 expressed sucrase-isomaltase, an enterocyte-specific gene which is a well-

7 Both sucrase isomaltase and alkaline phosphatase (a GPI-anchored prot

8 ional brush-border enzymes (lactase, sucrase-isomaltase and dipeptidyl peptidase 4) and visible subep

9 ion factors regulating expression of sucrase-isomaltase and fatty acid-binding protein.

10 Sucrase-isomaltase and lactase-phlorizin hydrolase expressions c

11 ionship of these nuclear proteins to sucrase-isomaltase and lactase-phlorizin hydrolase gene expressi

12 ne shows heterogeneous expression of sucrase-isomaltase and most lectin receptors.

13 and also a strong inhibitor of glucoamylase, isomaltase, and alpha-glucosidase.

14 erminal differentiation markers ITF, sucrase-isomaltase, and the mucin gene MUC2.

15 atalytic sites identical to those of sucrase-isomaltase, but the proteins are only 59% homologous.

16 40% (11%), SLFN12 by 61% (14%), and sucrase-isomaltase by 28% (8%) (n = 6, P < .05 for all).

17 ing sites were present in intestinal sucrase isomaltase, cdx-2 homeodomain protein, and intestinal fa

18 ate malabsorption was discovered: in sucrase-isomaltase deficiency, the enzyme fails to anchor in the

19 SIF1-binding proteins may regulate sucrase-isomaltase expression during postnatal development, but

20 The sucrose isomaltase gene (SI), is expressed exclusively in the in

21 e SIF1 cis-regulatory element of the sucrase-isomaltase gene and to the CE-LPH1 cis-regulatory elemen

22 The sucrase-isomaltase gene promoter has multiple regulatory element

23 with a protein-binding motif in the sucrase-isomaltase gene promoter, competition assays, and antibo

24 ytic differentiation markers villin, sucrase-isomaltase, glucose transporter 2 (GLUT2), and dipeptidy

25 he heterologously expressed protein, sucrase-isomaltase is a cAMP-dependent epithelial chloride chann

26 as found in suckling animals without sucrase-isomaltase messenger RNA (mRNA), and a higher-molecular-

27 inhibits beta-glucosidase, glucoamylase, and isomaltase more strongly than 1-deoxynojirimycin where t

28 in older animals with expression of sucrase-isomaltase mRNA.

29 drolases dipeptidyl-peptidase IV and sucrase-isomaltase or with binding of 10 of the 12 lectins teste

30 ver, crystallographic structural analysis of isomaltase predicts that another aspartic acid residue f

31 and inhibits transactivation of the sucrase-isomaltase promoter by Cdx-2.

32 A critical factor in regulating the sucrase-isomaltase promoter is Cdx2, an intestine-specific homeo

33 proteins are subunits of the rabbit sucrase-isomaltase protein (SI) complex.

34 Brush-border sucrase-isomaltase (SI) activity is complementary, through diges

35 cell differentiation, expression of sucrase isomaltase (SI) and dipeptidyl-peptidase IV (DPP-IV), tw

36 The mouse sucrase-isomaltase (SI) gene is an enterocyte-specific gene expr

37 The sucrase-isomaltase (SI) gene, which encodes an enterocyte brush

38 -dependent integral membrane protein sucrase-isomaltase (SI) in the Caco2 intestinal epithelial cell

39 Sucrase-isomaltase (SI) is an intestinal membrane-associated alp

40 Sucrase isomaltase (SI), a transmembrane disaccharidase found in

41 Sucrase-isomaltase (SI), an intestine-specific gene, is induced

42 Sucrase-isomaltase (SI), the product of an enterocyte-specific g

43 ids showed 100% homology with rabbit sucrase-isomaltase (SI).

44 ses, maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI).

45 proteins 1, 2, 3, 4, 5, 13, and 14; sucrase isomaltase (SI); dipeptidyl peptidase 4 (Dpp4); glucose

46 The brush border enzymes DPPIV and sucrase-isomaltase still correctly localize at the apical plasma

47 homologous functional subunits (sucrase and isomaltase) that both belong to the glycoside hydrolase

48 sialoglycoprotein receptor subunits, sucrase-isomaltase, the erythropoietin receptor, and two of the

49 analysis of the in vitro-translated sucrase-isomaltase was indistinguishable from that of the protei

50 A transmembrane apical protein, sucrase isomaltase, was found mispolarized in a subpopulation of