Isolation and partial characterization of SSI-like protease inhibitors from Streptomyces.
We attempted to screen a series of Streptomyces subtilisin inhibitor-like (SIL) proteins among several Streptomyces strains by using a highly sensitive assay system established by us. Of six randomly tested strains, four were found to produce SIL inhibitors as their major secreted proteins, suggesting that they might be distributed in a high frequency among this genus. Three inhibitors exhibited inhibition of both subtilisin BPN' and trypsin. Comparison of the amino terminal sequences of these isolated proteins with those of other reported SIL inhibitors revealed that the beta 1- and beta 2-sheets in SSI were highly conserved.
Taguchi
S
S
Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan.
Kojima
S
S
Kumagai
I
I
Ogawara
H
H
Miura
K
K
Momose
H
H
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D003429:Cross Reactions; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D015842:Serine Proteinase Inhibitors / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D013045:Species Specificity; D013302:Streptomyces / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D013381:Subtilisins / Q000037:antagonists & inhibitors
D001426:Bacterial Proteins; D015842:Serine Proteinase Inhibitors; C018150:subtilisin inhibitor protein, Streptomyces; D013381:Subtilisins