A Proteolytic Enzyme of Streptomyces Griseus

1959 ◽  
Vol 46 (5) ◽  
pp. 653-667 ◽  
Author(s):  
Masao Nomoto ◽  
Yoshiko Narahashi
Development ◽  
1972 ◽  
Vol 28 (1) ◽  
pp. 77-86
Author(s):  
J. Born ◽  
H. Tiedemann ◽  
H. Tiedemann

A naturally occurring inhibitor for the vegetalizing inducing factor has been incubated with different enzymes. Pancreatic ribonuclease, ribonuclease-T1, deoxyribunuclease, neuraminidase as well trypsin and papain diminish the inhibitor only very slightly or not at all. Pronase, a proteolytic enzyme from Streptomyces griseus inactivates the inhibitor completely.


1960 ◽  
Vol 48 (3) ◽  
pp. 453-462 ◽  
Author(s):  
MASAO NOMOTO ◽  
YOSHIKO NARAHASHI ◽  
MITSURU MURAKAMI

1960 ◽  
Vol 48 (4) ◽  
pp. 593-602 ◽  
Author(s):  
MASAO NOMOTO ◽  
YOSHIKO NARAHASHI ◽  
MITSURU MURAKAMI

1960 ◽  
Vol 48 (6) ◽  
pp. 906-918 ◽  
Author(s):  
MASAO NOMOTO ◽  
YOSHIKO NARAHASHI ◽  
MITSURU MURAKAMI

1970 ◽  
Vol 24 (03/04) ◽  
pp. 325-333 ◽  
Author(s):  
G. H Tishkoff ◽  
L. C Williams ◽  
D. M Brown

SummaryAs a corollary to our previous studies with bovine prothrombin, we have initiated a study of human prothrombin complex. This product has been isolated in crystalline form as a barium glycoprotein interaction product. Product yields were reduced compared to bovine product due to the increased solubility of the barium glycoprotein interaction product. On occasion the crystalline complex exhibited good yields. The specific activity of the crystalline complex was 1851 Iowa u/mg. Further purification of human prothrombin complex was made by removal of barium and by chromatography on Sephadex G-100 gels. The final product evidenced multiple procoagulant activities (II, VII, IX and X). The monomeric molecular weight determined by sedimentation equilibrium in a solvent of 6 M guanidine-HCl and 0.5% mercaptoethanol was 70,191 ± 3,057 and was homogeneous with respect to molecular weight. This product was characterized in regard to physical constants and chemical composition. In general, the molecular properties of human prothrombin complex are very similar to the comparable bovine product. In some preparations a reversible proteolytic enzyme inhibitor (p-aminophenylarsonic acid) was employed in the ultrafiltration step of the purification scheme to inhibit protein degradation.


2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Nicole Danielle Osier ◽  
George M Garrity ◽  
Dorothea Taylor
Keyword(s):  

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