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

Sjostrom, H. and Noren, O. and Christiansen, L. A. and Wacker, H. and Spiess, Martin and Biglermeier, B. and Rickli, E. E. and Semenza, G.. (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, 148 (2). pp. 321-325.

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Official URL: http://edoc.unibas.ch/45487/

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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 M r 260 000–265 000. 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 in 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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Spiess)
UniBasel Contributors:Spiess, Martin
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:0014-5793
e-ISSN:1873-3468
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:20 Nov 2017 10:16
Deposited On:20 Nov 2017 10:16

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