Boehringer Mannheim Gmbh

Roche Diagnostics Gmbh

Karl-Peter Hopfner

Erhard Kopetzki

Robert Huber

Richard Engh

Wolfram Bode

A chimeric serine protease whose protease domain is composed of two domain halves (half-sides) with a &bgr;-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.

Chimeric serine proteases

The invention relates to a non-glycosylated protein with enzymatic and serin protease activity, the zymogenous form thereof comprising the following domains of a protease of the factor IX family: (a) a catalytic domain, N-terminal bonded with (b) a zymogenous activation domain, N terminal bonded with (c) a EGF1 and/or EGF2 domain. Said protein can be used in a same way as the natural serine proteases of the factor IX family.

Recombinant blood-coagulation proteases

A chimeric serine protease whose protease domain is composeD. of two domain halves (half-sides) with a &bgr;-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.

A chimeric serine protease whose protease domain is composed of two domain halves (half-sides) with a .beta.-folded sheet structure, wherein the first domain half corresponds to the first domain half of a first serine protease and the second domain half corresponds to the second domain half of a second serine protease, has improved properties and can be readily crystallized.

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Munich, Germany

Karl-Peter Hopfner