PMID: 7152027Nov 8, 1982

N-Terminal sequences of pig intestinal sucrase-isomaltase and pro-sucrase--isomaltase. Implications for the biosynthesis and membrane insertion of pro-sucrase--isomaltase

FEBS Letters
H SjöströmG Semenza

Abstract

The hog sucrase-isomaltase complex is anchored to the small-intestinal brush border membrane, as in the rabbit, via a hydrophobic segment located in the N-terminal region of the isomaltase subunit. The immediate precursor of the 'final' sucrase-isomaltase (i.e., pro-sucrase-isomaltase as prepared from adult hogs whose pancreas had been disconnected from the duodenum) is an amphiphilic single polypeptide chain of Mr 260000-265000. Its N-terminal sequence is virtually identical with (not merely homologous to) the corresponding region of the isomaltase subunit of 'final' sucrase-isomaltase. This shows that the isomaltase portion of pro-sucrase-isomaltase is the N-terminal 'half' of the precursor polypeptide chain. Thus the succession of domains in pro-sucrase-isomaltase and its mode of anchoring in the membrane could be deduced. On this basis a likely mechanism of biosynthesis and insertion is proposed.

References

Oct 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H P HauriK J Isselbacher
Jan 1, 1978·Annual Review of Biochemistry·J M DiRienzoM Inouye
Jun 1, 1979·European Journal of Biochemistry·G von Heijne, C Blomberg
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Citations

Nov 1, 1983·Developmental Biology·R K MontgomeryB T Smith
Jan 1, 1985·Comparative Biochemistry and Physiology. A, Comparative Physiology·A Ozols, T Sheshukova
Jan 1, 1988·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·C Martínez del Rio, B R Stevens
Jan 1, 1983·CRC Critical Reviews in Biochemistry·H Hauser, G Semenza
Jan 1, 1995·Critical Reviews in Biochemistry and Molecular Biology·E H Van BeersJ Dekker

Related Concepts

Plasma Membrane
Enzyme Precursors
Intestines, Small
Microvilli
Multienzyme Complexes
Sucrase-Isomaltase Complex

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