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Purification and Characterization of Serine Proteinase 2 from Bacillus intermedius 3-19
A proteinase secreted in the late stationary phase was isolated from the culture fluid of Bacillus intermedius 3-19 by ion-exchange chromatography on CM-cellulose followed by FPLC on a Mono S column.Expand
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Coumarins from the roots and epigeal mass ofPrangos acaulis
We have studied for the first time the qualitative composition of the coumarins of the roots and epigeal mass of Pran~os acaulis (DC.) Bornm. collected in the fruit-bearing stage in the environs ofExpand
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Proteinases from Bacillus intermedius secreted in the late stages of sporulation.
BACKGROUND Proteinases are widely used in various fields of medicine, such as the treatment of burns, purulent wounds, or decubitus ulcers. On the basis of new microbial proteinases produced byExpand
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Coumarins from the roots ofPrangos arcis-romanae
atoms with hydroxy groups (singlets at 1.22 and 1.48 ppm, 3 H each, and 1.44 ppm, 6 H) and of a Ar-O-CH2--CH--grouping (multiplet at 4.20-4.51 ppm, 3 H). These facts agree completely with theExpand
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Subcellular localization, substrate specificity and crystallization of duodenase, a potential activator of enteropeptidase.
Duodenase, a serine protease from bovine duodenum mucosa, was located in endoplasmic reticulum, the Golgi secretory granules of epithelial cells and ducts of Brunner's glands by the A-goldExpand
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Activation of recombinant proenteropeptidase by duodenase
Duodenase, a serine proteinase from bovine Brunner's (duodenal) glands that was predicted to be a natural activator of enteropeptidase zymogen, cleaves and activates recombinant single‐chain bovineExpand
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Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type.
The interaction between duodenase, which belongs to a group of Janus-faced proteinases, and classical Bowman--Birk (BBI) and Kunitz (STI) type inhibitors from soybean was investigated. Duodenase wasExpand
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A serine protease from the bovine duodenal mucosa, chymotrypsin-like duodenase.
Chymotrypsin-like duodenase (ChlD), a new protease from the bovine duodenum mucosa was isolated and purified. The enzyme molecule is a single chain (25 kDa); the native enzyme is a monomer with anExpand
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Cloning and Molecular Modeling of Duodenase with Respect to Evolution of Substrate Specificity within Mammalian Serine Proteases That Have Lost a Conserved Active-Site Disulfide Bond
Mammalian serine proteases such as the chromosome 14 (Homo sapiens, Mus musculus) located granzymes, chymases, cathepsin G, and related enzymes including duodenase collectively represent a specialExpand
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Isolation and Characterization of Glutamyl Endopeptidase 2 from Bacillus intermedius 3-19
The culture filtrate of Bacillus intermedius 3-19 was used for isolation by chromatography on CM-cellulose and Mono S columns of a proteinase that is secreted during the late stages of growth. TheExpand
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