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EC Number
BRENDA No.
Title
Journal
Volume
Pages
Year
Organism
PubMed ID
3.4.21.66
29547
Affinity chromatography of thermitase
J. Appl. Biochem.
2
342-345
1980
Thermoactinomyces vulgaris
-
3.4.21.66
29544
Calcium ion binding by thermitase
FEBS Lett.
253
83-87
1989
Thermoactinomyces vulgaris
-
3.4.21.66
29533
Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin- type proteinases
FEBS Lett.
183
195-200
1985
Thermoactinomyces vulgaris
-
3.4.21.66
29554
Purification by affinity chromatography and characterization of two stable thermitase inhibitors from potatoes
Nahrung
32
91-107
1988
Thermoactinomyces vulgaris
-
3.4.21.66
29557
Thermitase from Thermoactinomyces vulgaris; amino acid sequence of the large N-terminal cyanogen bromide peptide
Collect. Czech. Chem. Commun.
50
885-896
1985
Thermoactinomyces vulgaris
-
3.4.21.66
29542
Use of microbial peptide inhibitors for characterization of the substrate specificity of thermitase, a thermostable serine protease from Thermoactinomyces vulgaris
Curr. Microbiol.
11
317-320
1984
Thermoactinomyces vulgaris
-
3.4.21.66
29565
Characterization of a protease from Thermoactinomyces vulgaris (thermitase). 3. Substrate specificity and properties of partially purified thermitase
Acta Biol. Med. Ger.
37
1205-1214
1978
Thermoactinomyces vulgaris
34957
3.4.21.66
29566
Characterization of a protease from Thermoactinomyces vulgaris (thermitase). 1. Purification of thermitase
Acta Biol. Med. Ger.
37
1185-1192
1978
Thermoactinomyces vulgaris
749455
3.4.21.66
29550
Characterization of a protease from Thermoactinomyces vulgaris (thermitase). 2. Single-step fine purification and protein-chemical characterization
Acta Biol. Med. Ger.
37
1193-1204
1978
Thermoactinomyces vulgaris
749456
3.4.21.66
29551
Effects of eglin-c binding to thermitase: three-dimensional structure comparison of native thermitase and thermitase eglin-c complexes
Proteins Struct. Funct. Genet.
12
63-74
1992
Thermoactinomyces vulgaris
1553381
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