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Structural basis of the activation and action of trypsin (1978)

Huber, Robert ; Bode, Wolfram

s.l. : American Chemical Society

Accounts of chemical research 11 (1978), S. 114-122

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ISSN: 1520-4898

Source: ACS Legacy Archives

Topics: Chemistry and Pharmacology

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1021/ar50123a006

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Aktivierung, Aktivität und Inhibierung des Rindertrypsins (1979)

Bode, Wolfram

Springer

Naturwissenschaften 66 (1979), S. 251-258

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ISSN: 1432-1904

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General

Notes: Abstract Trypsin is a prototype of a large group of enzymes belonging to serine proteinases. The X-ray crystal-structure analyses of its proenzyme trypsinogen, of the active trypsin and of their complexes formed with the pancreatic trypsin inhibitor (PTI) have considerably enhanced our understanding of the mechanisms of activitation, action and inhibition. The trypsinogen is an incompletely folded molecule. Its substrate-binding site becomes only completely fixed upon the enzymatic cleavage of an N-terminal peptide. The contact regions of trypsin and PTI are almost complementary. The complex formed is a (stable) intermediate in the normal tryptic substrate-cleavage reaction.