Some Properties of Luminal Sucrase and Sucrase-Isomaltase Complex in Rat Small Intestine
Some properties of luminal sucrase4somaltase complex and the effect of luminal fluid on their complex were studied in rat small intestine. Luminal contents were collected by flushing the small intestine with the buffered solution. The enzyme activity was observed in luminal contents and intestinal m...
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| Published in | Journal of Nutritional Science and Vitaminology Vol. 31; no. 2; pp. 243 - 252 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Japan
Center for Academic Publications Japan
01.01.1985
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0301-4800 1881-7742 |
| DOI | 10.3177/jnsv.31.243 |
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| Abstract | Some properties of luminal sucrase4somaltase complex and the effect of luminal fluid on their complex were studied in rat small intestine. Luminal contents were collected by flushing the small intestine with the buffered solution. The enzyme activity was observed in luminal contents and intestinal mucosa. Sucrase and Isomaltase activities were located mainly in the intestinal mucosa. However, approximately 20% of sucrase and 10% of isomaltase activities of total small intestine were found in the luminal contents. A significant amount of sucrase without isomaltase activity, the molecular weight of which was estimated at about 140, 000 daltons, was found in the luminal supernatant of the distal intestine in addition to the complexed form of sucrase and isomaltase. The luminal sucrase and sucrase-isomaltase complex had similar properties such as Km values, optimal pH, molecular weights and antigenicity against anti sucrase-isomaltase antibody compared with brush border membrane-bound sucrase-isomaltase complex. Furthermore, the supernatant of the luminal contents of the ileum had a degradative effect on the isomaltase moiety of the purified sucrase-isomaltase complex and a free sucrase without isomaltase also appeared in vitro as observed in vivo. These results suggest that the sucrase-isomaltase complex is released into the intestinal lumen from the brush border membrane and that a luminal factor affects the degradation step of this enzyme as well as the biosynthesis of su-crase-isomaltase complex. |
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| AbstractList | Some properties of luminal sucrase-isomaltase complex and the effect of luminal fluid on their complex were studied in rat small intestine. Luminal contents were collected by flushing the small intestine with the buffered solution. The enzyme activity was observed in luminal contents and intestinal mucosa. Sucrase and isomaltase activities were located mainly in the intestinal mucosa. However, approximately 20% of sucrase and 10% of isomaltase activities of total small intestine were found in the luminal contents. A significant amount of sucrase without isomaltase activity, the molecular weight of which was estimated at about 140,000 daltons, was found in the luminal supernatant of the distal intestine in addition to the complexed form of sucrase and isomaltase. The luminal sucrase and sucrase-isomaltase complex had similar properties such as Km values, optimal pH, molecular weights and antigenicity against anti sucrase-isomaltase antibody compared with brush border membrane-bound sucrase-isomaltase complex. Furthermore, the supernatant of the luminal contents of the ileum had a degradative effect on the isomaltase moiety of the purified sucrase-isomaltase complex and a free sucrase without isomaltase also appeared in vitro as observed in vivo. These results suggest that the sucrase-isomaltase complex is released into the intestinal lumen from the brush border membrane and that a luminal factor affects the degradation step of this enzyme as well as the biosynthesis of sucrase-isomaltase complex.Some properties of luminal sucrase-isomaltase complex and the effect of luminal fluid on their complex were studied in rat small intestine. Luminal contents were collected by flushing the small intestine with the buffered solution. The enzyme activity was observed in luminal contents and intestinal mucosa. Sucrase and isomaltase activities were located mainly in the intestinal mucosa. However, approximately 20% of sucrase and 10% of isomaltase activities of total small intestine were found in the luminal contents. A significant amount of sucrase without isomaltase activity, the molecular weight of which was estimated at about 140,000 daltons, was found in the luminal supernatant of the distal intestine in addition to the complexed form of sucrase and isomaltase. The luminal sucrase and sucrase-isomaltase complex had similar properties such as Km values, optimal pH, molecular weights and antigenicity against anti sucrase-isomaltase antibody compared with brush border membrane-bound sucrase-isomaltase complex. Furthermore, the supernatant of the luminal contents of the ileum had a degradative effect on the isomaltase moiety of the purified sucrase-isomaltase complex and a free sucrase without isomaltase also appeared in vitro as observed in vivo. These results suggest that the sucrase-isomaltase complex is released into the intestinal lumen from the brush border membrane and that a luminal factor affects the degradation step of this enzyme as well as the biosynthesis of sucrase-isomaltase complex. Some properties of luminal sucrase-isomaltase complex and the effect of luminal fluid on their complex were studied in rat small intestine. Luminal contents were collected by flushing the small intestine with the buffered solution. The enzyme activity was observed in luminal contents and intestinal mucosa. Sucrase and isomaltase activities were located mainly in the intestinal mucosa. However, approximately 20% of sucrase and 10% of isomaltase activities of total small intestine were found in the luminal contents. A significant amount of sucrase without isomaltase activity, the molecular weight of which was estimated at about 140,000 daltons, was found in the luminal supernatant of the distal intestine in addition to the complexed form of sucrase and isomaltase. The luminal sucrase and sucrase-isomaltase complex had similar properties such as Km values, optimal pH, molecular weights and antigenicity against anti sucrase-isomaltase antibody compared with brush border membrane-bound sucrase-isomaltase complex. Furthermore, the supernatant of the luminal contents of the ileum had a degradative effect on the isomaltase moiety of the purified sucrase-isomaltase complex and a free sucrase without isomaltase also appeared in vitro as observed in vivo. These results suggest that the sucrase-isomaltase complex is released into the intestinal lumen from the brush border membrane and that a luminal factor affects the degradation step of this enzyme as well as the biosynthesis of sucrase-isomaltase complex. Some properties of luminal sucrase4somaltase complex and the effect of luminal fluid on their complex were studied in rat small intestine. Luminal contents were collected by flushing the small intestine with the buffered solution. The enzyme activity was observed in luminal contents and intestinal mucosa. Sucrase and Isomaltase activities were located mainly in the intestinal mucosa. However, approximately 20% of sucrase and 10% of isomaltase activities of total small intestine were found in the luminal contents. A significant amount of sucrase without isomaltase activity, the molecular weight of which was estimated at about 140, 000 daltons, was found in the luminal supernatant of the distal intestine in addition to the complexed form of sucrase and isomaltase. The luminal sucrase and sucrase-isomaltase complex had similar properties such as Km values, optimal pH, molecular weights and antigenicity against anti sucrase-isomaltase antibody compared with brush border membrane-bound sucrase-isomaltase complex. Furthermore, the supernatant of the luminal contents of the ileum had a degradative effect on the isomaltase moiety of the purified sucrase-isomaltase complex and a free sucrase without isomaltase also appeared in vitro as observed in vivo. These results suggest that the sucrase-isomaltase complex is released into the intestinal lumen from the brush border membrane and that a luminal factor affects the degradation step of this enzyme as well as the biosynthesis of su-crase-isomaltase complex. |
| Author | ABE, Masako YAMADA, Kazuhiko MORIUCHI, Sachiko HOSOYA, Norimasa |
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| References | 15) Hedrick, J. L., and Smith, A. J. (1968): Size and charge isomer separation and es- timation of molecular weights of proteins by disc gel electrophoresis. Arch. Biochem. Biophys., 126, 155-164. 7) Hauri, H., Quaroni, A., and Isselbacher, K. J. (1979): Biogenesis of intestinal plasma membrane posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA., 76, 5183-5186. 8) Riepe; S. P., Goldstein, J., and Alper, D. H. (1980): Effect of secreted bacteroides proteases on human intestinal brush border hydrolases. J. Clin. Invest., 60, 314-322. 4) Sasaki, M., Yamada, K., Moriuchi, S., and Hosoya, N. (1979): Purification and characterization of rat intestinal sucrase-isomaltase complex. Eiyo to Shokuryo (J. Jpn. Soc. Food and Nutr.), 32, 201-208. 16) Dahlqvist, A. (1964): Method for assay of intestinal disaccharidases. Anal. Biochem., 7, 18-25. 21) Quastler, H., and Sherman, F. G. (1959): Cell population kinetics in the intestinal epithelium of the mouse. Exp. Cell. Res., 17, 420-438. 23) Alpers, D. H., and Tedesco, F. J. (1975): The possible role of pancreatic proteases in the turnover of intestinal brush border proteins. Biochim. Biophys. Acta, 401, 28-40. 24) Olsen, W. A., and Korsmo, H. A. (1982): Sucrase metabolism in germfree rats. Am. J. Physiol., 242, G650-G653. 22) Alpers, D. H. (1972): The relation of size to the relation rates of degradation of intestinal brush border proteins. J. Clin. Invest., 51, 2621-2630. 14) Faye, L. (1981): A new enzymatic staining method for the detection of radish β- fructosidase in gel electrophoresis. Anal. Biochem., 112, 90-95. 19) Aramayo, L. A., de Silvia, D. G. H., Hughes, C. A., Brown, G. A., and Mcneish, A. S. (1983): Disaccharidase activities in jejunal fluid. Arch. Disease Childhood, 58, 686-691. 5) Mizuno, K., Moriuchi, S., and Hosoya, N. (1982): Demonstration of sucrase- isomaltase complex in chick intestine. J. Nutr. Sci. Vitaminol., 28, 599-608. 13) Davis, B. J. (1964): Disc electrophoresis-II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci., 121, 404-427. 1) Kolinska, J., and Semenza, G. (1967): Studies on intestinal sucrase and on intestinal sugar transport. V. Isolation and properties of sucrase-isomaltase from rabbit small intestine. Biochim. Biophys. Acta, 146, 181-195. 10) Lorenzsonn, V., and Olsen, W. A. (1982): In vivo responses of rat intestinal epithelium to intraluminal dietary lectins. Gastroenterology, 82, 838-848. 20) Leblond, C. P., and Stevens, C. E. (1948): The constant renewal of intestinal epithelium in the albino rat. Anat. Rec., 100, 357-377. 3) Sjostrom, H., Noren, O., Christiansen, L. A., Wacker, H., and Semenza, G. (1980): A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine, implications for the biosynthesis of a mammalian integral stalked membrane protein. J. Biol. Chem., 255, 11332-11338. 2) Conklin, K. A., Yamashiro, K. M., and Gray, G. H. (1975): Human intestinal sucrase-isomaltase; identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits. J. Biol. Chem., 250, 5735-5741. 11) Yamada, K., Moriuchi, S., and Hosoya, N. (1978): Developmental changes in the sucrase-isomaltase complex in the rat intestinal mucosa. J. Nutr. Sci. Vitaminol., 24, 177-184. 12) Yamada, K., Moriuchi, S., and Hosoya, N. (1979): Some characteristics of early appearing isomaltase in intestinal mucosa of suckling rat. J. Nutr. Sci. Vitaminol., 25, 543-552. 18) Berteloot, A., Chabot, J.G., and Hugon, J. S. (1981): Turnover of mouse intestinal brush border membrane proteins and enzymes in organ culture. A direct evaluation from studies on the evaluation of enzyme activities during the culture. Biochim. Biophys. Acta, 678, 423-436. 25) Senegas-Balas, F., Balas, D., and Ribet, A. (1981): Effect of pancreatic duct ligation on the hamster intestinal mucosa. Variation of several hydrolases. Digestion, 21, 83-91. 9) Vasseur, M., Ferard, G., and Pousse, A. (1978): Rat intestinal brush border enzymes release by deoxycholate in vivo. Pflugers Arch., 373, 133-137. 17) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951): Protein measurement with the folin phenol reagent. J. Biol. Chem., 193, 265-275. 6) Hauri, H., Wacker, H., Rickli, E., Bigler-Meier, B., Quaroni, A., and Semenza, G. (1982): Biosynthesis of sucrase-isomaltase. Purification and NH2-terminal amino acid sequence of the rat sucrase-isomaltase precursor (pro-sucrase-isomaltase) from fetal intestinal transplants. J. Biol. Chem., 257, 4522-4528. |
| References_xml | – reference: 21) Quastler, H., and Sherman, F. G. (1959): Cell population kinetics in the intestinal epithelium of the mouse. Exp. Cell. Res., 17, 420-438. – reference: 17) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951): Protein measurement with the folin phenol reagent. J. Biol. Chem., 193, 265-275. – reference: 2) Conklin, K. A., Yamashiro, K. M., and Gray, G. H. (1975): Human intestinal sucrase-isomaltase; identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits. J. Biol. Chem., 250, 5735-5741. – reference: 8) Riepe; S. P., Goldstein, J., and Alper, D. H. (1980): Effect of secreted bacteroides proteases on human intestinal brush border hydrolases. J. Clin. Invest., 60, 314-322. – reference: 24) Olsen, W. A., and Korsmo, H. A. (1982): Sucrase metabolism in germfree rats. Am. J. Physiol., 242, G650-G653. – reference: 20) Leblond, C. P., and Stevens, C. E. (1948): The constant renewal of intestinal epithelium in the albino rat. Anat. Rec., 100, 357-377. – reference: 18) Berteloot, A., Chabot, J.G., and Hugon, J. S. (1981): Turnover of mouse intestinal brush border membrane proteins and enzymes in organ culture. A direct evaluation from studies on the evaluation of enzyme activities during the culture. Biochim. Biophys. Acta, 678, 423-436. – reference: 14) Faye, L. (1981): A new enzymatic staining method for the detection of radish β- fructosidase in gel electrophoresis. Anal. Biochem., 112, 90-95. – reference: 13) Davis, B. J. (1964): Disc electrophoresis-II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci., 121, 404-427. – reference: 9) Vasseur, M., Ferard, G., and Pousse, A. (1978): Rat intestinal brush border enzymes release by deoxycholate in vivo. Pflugers Arch., 373, 133-137. – reference: 22) Alpers, D. H. (1972): The relation of size to the relation rates of degradation of intestinal brush border proteins. J. Clin. Invest., 51, 2621-2630. – reference: 3) Sjostrom, H., Noren, O., Christiansen, L. A., Wacker, H., and Semenza, G. (1980): A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine, implications for the biosynthesis of a mammalian integral stalked membrane protein. J. Biol. Chem., 255, 11332-11338. – reference: 23) Alpers, D. H., and Tedesco, F. J. (1975): The possible role of pancreatic proteases in the turnover of intestinal brush border proteins. Biochim. Biophys. Acta, 401, 28-40. – reference: 7) Hauri, H., Quaroni, A., and Isselbacher, K. J. (1979): Biogenesis of intestinal plasma membrane posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA., 76, 5183-5186. – reference: 16) Dahlqvist, A. (1964): Method for assay of intestinal disaccharidases. Anal. Biochem., 7, 18-25. – reference: 1) Kolinska, J., and Semenza, G. (1967): Studies on intestinal sucrase and on intestinal sugar transport. V. Isolation and properties of sucrase-isomaltase from rabbit small intestine. Biochim. Biophys. Acta, 146, 181-195. – reference: 5) Mizuno, K., Moriuchi, S., and Hosoya, N. (1982): Demonstration of sucrase- isomaltase complex in chick intestine. J. Nutr. Sci. Vitaminol., 28, 599-608. – reference: 10) Lorenzsonn, V., and Olsen, W. A. (1982): In vivo responses of rat intestinal epithelium to intraluminal dietary lectins. Gastroenterology, 82, 838-848. – reference: 19) Aramayo, L. A., de Silvia, D. G. H., Hughes, C. A., Brown, G. A., and Mcneish, A. S. (1983): Disaccharidase activities in jejunal fluid. Arch. Disease Childhood, 58, 686-691. – reference: 25) Senegas-Balas, F., Balas, D., and Ribet, A. (1981): Effect of pancreatic duct ligation on the hamster intestinal mucosa. Variation of several hydrolases. Digestion, 21, 83-91. – reference: 11) Yamada, K., Moriuchi, S., and Hosoya, N. (1978): Developmental changes in the sucrase-isomaltase complex in the rat intestinal mucosa. J. Nutr. Sci. Vitaminol., 24, 177-184. – reference: 15) Hedrick, J. L., and Smith, A. J. (1968): Size and charge isomer separation and es- timation of molecular weights of proteins by disc gel electrophoresis. Arch. Biochem. Biophys., 126, 155-164. – reference: 6) Hauri, H., Wacker, H., Rickli, E., Bigler-Meier, B., Quaroni, A., and Semenza, G. (1982): Biosynthesis of sucrase-isomaltase. Purification and NH2-terminal amino acid sequence of the rat sucrase-isomaltase precursor (pro-sucrase-isomaltase) from fetal intestinal transplants. J. Biol. Chem., 257, 4522-4528. – reference: 12) Yamada, K., Moriuchi, S., and Hosoya, N. (1979): Some characteristics of early appearing isomaltase in intestinal mucosa of suckling rat. J. Nutr. Sci. Vitaminol., 25, 543-552. – reference: 4) Sasaki, M., Yamada, K., Moriuchi, S., and Hosoya, N. (1979): Purification and characterization of rat intestinal sucrase-isomaltase complex. Eiyo to Shokuryo (J. Jpn. Soc. Food and Nutr.), 32, 201-208. |
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| SubjectTerms | Animals Chromatography, Gel Exudates and Transudates - enzymology intestinal lu-minal fluid Intestinal Mucosa - enzymology Intestinal Mucosa - metabolism Intestine, Small - enzymology Kinetics luminal sucrase Male Multienzyme Complexes - metabolism Rats Rats, Inbred Strains Sucrase - metabolism sucrase-isomaltase complex Sucrase-Isomaltase Complex - metabolism Tissue Distribution |
| Title | Some Properties of Luminal Sucrase and Sucrase-Isomaltase Complex in Rat Small Intestine |
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