Proteolytic enzymes from recombinant Streptomyces lividans TK24.

FEMS microbiology letters ·Vol. 53 ·No. 1-2 ·1989-11-00 ·Pages 31-5

Aretz W, Koller KP, Riess G

Abstract

Different proteases from the culture fluids of recombinant Streptomyces lividans strains were isolated. Several individual proteases were separated and characterized. A chymotrypsin-chylike activity (CLA) was identified that specifically degrades a fusion protein between the alpha-amylase inhibitor from S. tendae (Tendamistat, HOE467) and proinsulin from the monkey Macaca fascicularis. The effective chemical inhibition of the degrading enzyme is demonstrated.

MeSH Terms

Amino Acid Sequence Animals Bacterial Proteins/metabolism Chromatography, Ion Exchange Chymotrypsin/antagonists & inhibitors,metabolism Metals/pharmacology Molecular Sequence Data Peptide Hydrolases/isolation & purification,metabolism Recombinant Fusion Proteins/metabolism Streptomyces/enzymology,genetics,growth & development Time Factors

Chemicals

Bacterial Proteins Metals Recombinant Fusion Proteins Peptide Hydrolases Chymotrypsin

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Aretz W

Hoechst AG, Frankfurt/Main, F.R.G.

Koller K P

Riess G

Article Info

Journal

FEMS microbiology letters

Abbr.

FEMS Microbiol Lett

ISSN

0378-1097

DOI

10.1016/0378-1097(89)90361-3

Published

1989-11-00

Pages

31-5

Language

English

Region

England

NLM ID

7705721

Subset

External Links

PubMed source DOI: 10.1016/0378-1097(89)90361-3 View journal details

Analysis Services

Proteolytic enzymes from recombinant Streptomyces lividans TK24.

Contact

WeChat Official Account