Improvement of intact human lipocortin-I production in Saccharomyces cerevisiae by inhibiting proteolysis

4Citations
Citations of this article
4Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Human lipocortin-I (hLC1), when was expressed as a secretory product in Saccharomyces cerevisiae, was cleaved to a significant extent by endoproteolytic processing, resulting in the accumulation of des1-26-hLC1 in the culture supernatant. This proteolytic cleavage was inhibited significantly by the addition of high concentrations of L-arginine and L-lysine, with a resultant marked improvement in the yield of intact hLC1. When the hLC1 was expressed in S. cerevisiae mutants deficient in one or two of the following endoproteases, Kex2p, Mkc7p and Yps1p (Yap3p), the mutants exhibited no reduction in the extent of hLC1 proteolysis, indicating that these endoproteases are not involved in the proteolytic cleavage of hLC1.

Cite

CITATION STYLE

APA

Choi, W. A., Oh, G. H., Kang, H. A., & Chung, B. H. (2000). Improvement of intact human lipocortin-I production in Saccharomyces cerevisiae by inhibiting proteolysis. Journal of Bioscience and Bioengineering, 89(1), 77–80. https://doi.org/10.1016/S1389-1723(00)88054-8

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free