Does sucrase—isomaltase always exist as a complex in human intestine?

Skovbjerg, Hanne; Sjöström, Hans; Norén, Ove

doi:10.1016/0014-5793(79)80572-4

Cited by 11 publications

(4 citation statements)

References 12 publications

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“…Therefore, we considered this second antigen of sucraseisomaltase to be an intrinsic degradation product of sucrase-isomaltase in which the sucrase subunit has been at least partially broken down. The similar antigen of sucrase-isomaltase which lacks sucrase activity, but has isomaltase activity, has been reported in brush border membranes of human jejunum (Skovbjerg et al, 1979). The second antigen of sucrase-isomaltase is distinguishable from the main (intact) antigen by its faster anodal electrophoretic mobility (Fig.…”

Section: Discussionsupporting

confidence: 60%

Evidence of degradation process of sucrase-isomaltase in jejunum of adult rats

Goda¹,

Koldovský²

1985

Biochemical Journal

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To evaluate degradation processes of sucrase-isomaltase in adult rat jejunum, we determined enzymic activity of sucrase and isomaltase and compared it with the amount of immunoreactive sucrase-isomaltase. In rats fed or starved for 18h, killed at 10:00 h or 22:00 h, sucrase activity (expressed on the basis of total protein or of immunoreactive sucrase-isomaltase) was significantly (P less than 0.02) lower in the lower jejunum than in the upper jejunum; isomaltase activity was similar in both segments. Crossed immunoelectrophoresis demonstrated the existence of a second sucrase-isomaltase antigen reacting with anti-(sucrase-isomaltase) serum. This antigen was present in larger amounts in the lower jejunum than in the upper jejunum, exhibited immunological partial identity with the intact sucrase-isomaltase, and had isomaltase activity but no sucrase activity. Results suggest that this antigen is a degradation product of sucrase-isomaltase in which the sucrase active site has been broken down. To examine the role of pancreatic enzymes in degradation of sucrase-isomaltase, common pancreatico-biliary ducts were ligated. Within 18 h after the operation, the difference of sucrase activity between the upper and the lower jejunum disappeared and the amount of the second sucrase-isomaltase antigen markedly decreased in the lower jejunum. Our results indicate that, during the degradation of intestinal sucrase-isomaltase by the pancreatic proteinases, degradation of the sucrase active site precedes that of the isomaltase active site.

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Section: Discussionsupporting

confidence: 60%

Evidence of degradation process of sucrase-isomaltase in jejunum of adult rats

Goda¹,

Koldovský²

1985

Biochemical Journal

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“…and dipeptidyl peptidase 1V precipitates compared to a normal biopsy. As previously shown (25), normal jejunal biopsies contain a small amount of free isomaltase that in crossed immunoelectrophoresis interferes with the sucrase-isomaltase precipitate. The biopsy from patient 3 shows in crossed immunoelectrophoresis one precipitate (1) with a similar electrophoretic mobility and the same enzymatic staining properties as the free isomaltase precipitate in the normal biopsies (Fig.…”

Section: Fig I Rocket Immunoelectrophoresis After Staining With Comentioning

confidence: 56%

“…we recently demonstrated the presence of free isomaltase in addition to the sucrase-isomaltase in normal jejunal biopsies (25). In this paper.…”

mentioning

confidence: 52%

Immunoelectrophoretic Studies on Human Small Intestinal Brush Border Proteins. The Residual Isomaltase in Sucrose Intolerant Patients

Skovbjerg

Krasilnikoff

1981

Pediatr Res

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SummarySmall intestinal biopsies from three patients with sucrose intolerance (sucrase-isomaltase deficiency) were studied by means of immunoelectrophoresis and enzymatic assays. All patients lacked sucrase activity ( t l unit/g protein). One of the patients had a substantial isomaltase activity (7.8 unit/g protein). Immunoelectrophoresis revealed the presence of the isomaltase polypeptide of the sucrase-isomaltase in this patient. None of the biopsies showed any precipitate that might represent a modified inactive sucrase protein. SpeculationIt is probable that patients with sucrose intolerance constitute a heterogeneous group, with some of the patients lacking both sucrase and isomaltase activities whereas others have retained an active isomaltase polypeptide.

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“…Peroxidase conjugated swine immunoglobulins to rabbit immunoglobulins were obtained from Dako (Denmark) and Tween 20 from Merck (Munchen, F.R.G.). The other chemicals were obtained as previously described (6,9).…”

Section: Chemicalsmentioning

confidence: 99%

Maltase‐Glucoamylase and Residual Isomaltase in Sucrose Intolerant Patients

Skovbjerg,

Krasilnikoff

1986

J. pediatr. gastroenterol. nutr.

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Summary: Small intestinal biopsies from nine patients with sucrase‐isomaltase deficiency (sucrose‐intolerance) were analyzed. All patients lacked sucrase activity and three patients had a residual isomaltase activity and a corresponding isomaltase precipitate following immunoelectrophoresis. By polyacrylamide gel electrophoresis in sodium dodecyl sulfate followed by immunoblotting the residual isomaltase appeared as a single polypeptide with molecular weight of ∼145,000. Maltase‐glucoamylase in the biopsies was specifically quantitated by crossed immunoelectrophoresis. One of the patients had an almost total deficiency of maltase‐glucoamylase in the biopsy, three patients had a normal amount of maltase‐glucoamylase, and five patients constituted an intermediary group. These results indicate that some of the sucrase‐isomaltase deficient patients also have a more or less pronounced deficiency of maltase‐glucoamylase. The patients constitute an even more heterogeneous group than earlier suggested and should be classified by the amount not only of sucrase and isomaltase but also of maltase‐ glucoamylase.

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Does sucrase—isomaltase always exist as a complex in human intestine?

Cited by 11 publications

References 12 publications

Evidence of degradation process of sucrase-isomaltase in jejunum of adult rats

Evidence of degradation process of sucrase-isomaltase in jejunum of adult rats

Immunoelectrophoretic Studies on Human Small Intestinal Brush Border Proteins. The Residual Isomaltase in Sucrose Intolerant Patients

Maltase‐Glucoamylase and Residual Isomaltase in Sucrose Intolerant Patients

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