Human prourokinase mutants

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

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4351723, 435212, 435226, 4353201, C12N 972, C12N 1500

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050988409

ABSTRACT:
A human prourokinase mutant in which the entire or a partial epidermal growth factor domain of human prourokinase is deleted or a partial epidermal growth factor domain of human prourokinase is replaced by one or more different amino acid residues, said mutant having a longer blood half-life than naturally occurring human prourokinase while retaining prourokinase enzymatic activity. In this human prourokinase mutant the region selected from the group consisting of: (a) from asparagine (10) to cysteine (42); (b) from asparagine (10) to aspartic acid (45); and (c) from asparagine (10) to threonine (49) is missing.

REFERENCES:
Cell Structure and Function 10, 151-159 (1985) entitled "Thrombolytic Properties of an Inactive Proenzyme Form of Human Urokinase Secreted from Human Kidney Cells", pp. 151-159.
Hoppe-Seyler's Z. Physiol. Chem. Bd. 363, S.1155-1165, Oct. 1982 entitled "The Primary Structure of High Molecular Mass Urokinase from Human Urine the Complete Amino Acid Sequence of the A Chain".
The Journal of Biological Chemistry, vol. 260, No. 22, Issue of Oct. 5, pp. 12377-12381, 1985 entitled "Proteolytic Cleavage of Single-Chain Pro-Urokinase Induces Conformational Change . . .".
Communication, The Journal of Biological Chemistry, vol. 262, No. 10, Issue of Apr. 5, pp. 4437-4400 4440, 1987 entitled "The Receptor-Binding Sequence of Urokinase"; A Biological Function for the . . . .
Communication, The Journal of Biological Chemistry, vol. 263, No. 4, Issue of Feb. 5, pp. 1599-1602, 1988 entitled "A Tissue-Type Plasminogen Activator Mutant with Prolonged Clearance in vivo"; Effect of Removal of the Growth Factor Domain.
Kornfield et al., Ann. Rev. Biochem., 54, 631-634 (1985).

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