Kunitz domain polypeptide zkun10

Details Kunitz domain polypeptide zkun10 Kunitz domain polypeptide zkun10

2005-07-05

2005-07-05

Wax, Robert A. (Department: 1653)

Organic compounds -- part of the class 532-570 series

Organic compounds

Carbohydrates or derivatives

C435S069100, C435S320100, C435S252300, C435S325000, C435S018000

Reexamination Certificate

active

06914135

ABSTRACT:
Proteinase inhibitors comprising a Kunitz domain are disclosed. The Kunitz domain comprises a motif of amino acid residues as shown in SEQ ID NO:4, and the sequence of the Kunitz domain is shown in residues 57 through 107 of SEQ ID NO:2. The polypeptide also includes an N-terminal collagen domain in which a von Willebrand domain resides, and is shown in SEQ ID NO: 5. Also disclosed are methods for making the proteinase inhibitors, and expression vectors and cultured cells that are useful within the methods. The proteinase inhibitors may be used as components of cell culture media, in protein purification, and as inhibitors of protease degradation of plasma proteins.

REFERENCES:
INC527550, LIFESEQ™ Clone Information Results, Incyte Pharmaceuticals, Inc., 1999.
INC2763021, LIFESEQ™ Clone Information Results, Incyte Pharmaceuticals, Inc., 1999.
P15989, Doliana et al., 1990.
AAR81918, Ladner et al., 1996.
AA846371, Strausberg, 1998.
AQ141660, Mahairas et al., 1998.
Mayer et al.,European Journal of Biochemistry,225: 573-580, 1994.
Bonaldo et al.,J. Biol. Chem.264: 20235-20239, 1989.
Ngo et al., “Computational complexity protein structure prediction, and the levinthal paradox,”The Protein Folding Problem and Tertiary Structure Predictionpp. 491-495, Merz, Jr. K. et al. Eds. Birkhauser, Boston, 1994.
Qin et al., “Functional characterization of Kunitz domains in hepatocyte growth factor activator inhibitor type 2,”FEBS Letters436: 111-114, 1998.
Doerks et al., “Protein annotation: detective work for function prediction,”TIG14:248-250, 1998.

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