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Article

Expression, isolation and characterization of a mutated human plasminogen kringle 3 with a functional lysine binding site.

Cellular and molecular life sciences : CMLS - 1 Jan 1999

Bürgin J, Schaller J

Abstract excerpt

Each kringle of human plasminogen (HPg) except kringle 3 (K3) exhibits affinity for omega-aminocarboxylic acids. Assuming that the K3 domain contains a preformed but nonfunctional lysine binding site (LBS), Lys311 was altered by site-directed mutagenesis into Asp311 in accordance with the consensus sequence of the LBS. Cys297 involved in the interkringle disulfide bridge was mutated into Ser297 to minimize...

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Identifiers

PMID: 10065160
DOI: 10.1007/s000180050278
PMCID: PMC11146829

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Source receipt: pubmed, retrieved 7 Sept 2026.

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