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Article

Secretion of active kringle-2-serine protease in Escherichia coli.

Biochemistry - 16 Oct 1990

Obukowicz M G, Gustafson M E, Junger K D, Leimgruber R M, Wittwer A J, Wun T C, Warren T G, Bishop B F, Mathis K J, McPherson D T

Abstract excerpt

Active human tissue plasminogen activator variant kringle-2-serine protease (K2 + SP domains; referred to as MB1004) was synthesized as a secreted protein in Escherichia coli, isolated, and characterized. MB1004 is a relatively large and complex protein, approximately 38 kDa in size and containing nine disulfide bonds. MB1004 without a pro region was secreted into the periplasm of E. coli by fusing the protein to...

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PMID: 2125481
DOI: 10.1021/bi00493a033

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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