Literature DB >> 1236142

Tryptic digestion of native small-intestinal sucrase - isomaltase complex: isolation of the sucrase subunit.

A Quaroni, E Gershon-Quaroni, G Semenza.   

Abstract

Limited tryptic digestion of native sucrase - isomaltase complex produced a more rapid destruction of isomaltase activity than sucrase activity. It was possible to isolate a partially fragmented sucrase subunits in high yields with a specific activity twice that of the native complex. Amino acid and carbohydrate analyses are reported and compared with the results obtained for sucrase - isomaltase complex and isomaltase subunit obtained by a different method.

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Year:  1975        PMID: 1236142     DOI: 10.1111/j.1432-1033.1975.tb04017.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  3 in total

1.  Characterization of degradation process of sucrase-isomaltase in rat jejunum with monoclonal-antibody-based enzyme-linked immunosorbent assay.

Authors:  T Goda; A Quaroni; O Koldovský
Journal:  Biochem J       Date:  1988-02-15       Impact factor: 3.857

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

Authors:  T Goda; O Koldovský
Journal:  Biochem J       Date:  1985-08-01       Impact factor: 3.857

3.  Circadian rhythm of intestinal sucrase activity in rats. Mechanism of enzyme change.

Authors:  M A Kaufman; H A Korsmo; W A Olsen
Journal:  J Clin Invest       Date:  1980-05       Impact factor: 14.808

  3 in total

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