Abstract
Washed-cell suspensions of Bacillus amyloliquefaciens secrete significant amounts of the extracellular enzymes alpha-amylase and protease for about 15 min in the almost complete absence of protein synthesis. This apparently represents release of preformed enzyme en route to secretion. The release was independent of energy but was affected by temperature. Pulse-labeling experiments showed that newly synthesized enzyme molecules are either immediately released into the external medium or equilibrate with the preformed enzyme prior to eventual secretion. The results are compatible with a model of secretion whereby enzyme molecules emerging from the cell membrane become temporarily restricted by the cell wall so that a small pool of active enzyme accumulates in this region.
MeSH Terms
Amino Acids/metabolism
Amylases/biosynthesis,immunology,metabolism
Animals
Azides/pharmacology
Bacillus/enzymology,metabolism
Bacterial Proteins/biosynthesis
Cell Fractionation
Cell Wall/enzymology
Chloramphenicol/pharmacology
Dinitrophenols/pharmacology
Leucine/metabolism
Micropore Filters
Peptide Hydrolases/biosynthesis,immunology,metabolism
Phenylalanine/metabolism
Precipitin Tests
Rabbits/immunology
Temperature
Time Factors
gamma-Globulins
Chemicals
Amino Acids
Azides
Bacterial Proteins
Dinitrophenols
gamma-Globulins
Phenylalanine
Chloramphenicol
Amylases
Peptide Hydrolases
Leucine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gould A R
May B K
Elliott W H
References (8)
8 references, click to expand
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