Repression of the synthesis of exocellular and intracellular proteinases inBacillus megaterium
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Microbiology
Link
http://link.springer.com/content/pdf/10.1007/BF02875957.pdf
Reference10 articles.
1. Aiappa P.S., Lampen J.O.: Penicillinase-releasing protease ofBacillus licheniformis 749. Specificity for hydroxyamino acids.J. Biol. Chem. 252, 1745 (1977).
2. Bettinger G.E., Lampen J.O.: Evidence for the extrusion of an incompletely folded from penicillinase during secretion by protoplasts ofBacillus licheniformis 749/C.Biochem. Biophys. Res. Commun. 43, 200 (1971).
3. Blobel G., Lingappa V.R., Katz F.N., Lodish H.L.: A signal sequence for the insertion of a transmembrane glycoprotein. Similarity to the signals of secretory proteins in primary structure and function.J. Biol. Chem. 253, 8667 (1978).
4. Čechová J., Chaloupka J.: Functional half-life of the exocellular proteinase mRNA ofBacillus megaterium.Folia Microbiol. 23, 329 (1978).
5. Chaloupka J., Křečková P.: Regulation of the formation of protease inBacillus megaterium. I. The influence of amino acids on the enzyme formation.Folia Microbiol. 11, 82 (1966).
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